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Journal articles on the topic 'Antigenic determinants'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 July 2024

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1

Stephens, R. S., E. A. Wagar, and G. K. Schoolnik. "High-resolution mapping of serovar-specific and common antigenic determinants of the major outer membrane protein of Chlamydia trachomatis." Journal of Experimental Medicine 167, no. 3 (March 1, 1988): 817–31. http://dx.doi.org/10.1084/jem.167.3.817.

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The principal surface protein antigen of Chlamydia trachomatis is the major outer membrane protein (MOMP). The MOMP is antigenically complex. Among the 15 serovars of C. trachomatis, mAbs define serovar-, subspecies-, and species-specific determinants on MOMP. The molecular basis of the antigenic diversity of these proteins is reflected in amino acid variable sequence domains. We have mapped the dominant topographic antigenic determinants of MOMP that are defined by mAbs. Using recombinant DNA approaches we have identified the linear distribution of two antigenic domains. One domain contains a serovar-specific determinant and the other contains subspecies- and species-specific determinants. These antigenic domains correspond to two amino acid sequence variable domains. Synthetic peptides were immunogenic and these resolved the serovar-specific determinant within a 14-amino acid peptide. The subspecies- and species-specific determinants were overlapping within a 16-amino acid peptide.

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2

Appel, J. R., C. Pinilla, H. Niman, and R. Houghten. "Elucidation of discontinuous linear determinants in peptides." Journal of Immunology 144, no. 3 (February 1, 1990): 976–83. http://dx.doi.org/10.4049/jimmunol.144.3.976.

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Abstract Synthetic peptides, made by the method of simultaneous multiple peptide synthesis, were coupled to the protein carrier keyhole limpet hemocyanin and used to raise mAb. Omission and substitution analogs of the original peptides were tested by ELISA to characterize their reactivity with the respective mAb. Linear antigenic determinants were located for 18 different peptides by using omission analogs. The length of the antigenic determinants ranged from 2 to 8 residues, with an average of 6 residues. The three aromatic amino acids, phenylalanine, tryptophan, and tyrosine, the charged hydrophilic amino acids, aspartic acid and lysine, and the neutral amino acid alanine were found to occur most often in the determinant region of the peptides tested, whereas asparagine, cysteine, and histidine occurred the least often. Alanine substitution analogs provided more information than omission analogs by enabling the determination of which side chain groups of the antigenic determinant residues were not critical for binding to the mAb. Detailed, "fingerprint" information about the interaction of the peptide, GASPYPNLSNQQT, and its mAb was obtained by synthesizing a complete series of analogs with individual substitutions for each position of the antigenic determinant, PYPNLS, with the 19 other amino acids. These results suggest that, at the amino acid level, all antigenic determinants of synthetic peptides defined by mAb can be considered discontinuous linear determinants.

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3

Stolbikov, A. S., R. K. Salyaev, and N. I. Rekoslavskaya. "A bioinformatics approach for identifying the probable cause of the cross-interaction of antibodies to the antigenic protein HPV16 L1 with the HPV6 L1 protein." Vavilov Journal of Genetics and Breeding 25, no. 7 (December 3, 2021): 787–92. http://dx.doi.org/10.18699/vj21.090.

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This paper describes an attempt to analyze, with the aid of bioinformatics resources (programs and databases), the probable cause of the cross-interaction of antibodies against HPV16 L1 with antigenic protein HPV6 L1, which has been revealed in the investigation of the candidate vaccine obtained on the base of a plant expression system (tomato plants). In our opinion, the most likely reason for the cross-interaction of antibodies with antigens of different pathogenic HPV types is the similarity of their antigenic determinants. In this work, the amino acid sequences of HPV16 L1 and HPV6 L1 used for the development of a binary vaccine against cervical cancer and anogenital papillomatosis have been analyzed. For the analysis of antigenic determinants, the programs BepiPred-2.0: Sequential B-Cell Epitope Predictor, DiscoTope 2.0 Server and SYFPEITHI have been used. As a result of the analysis of probable B-cell linear determinants (epitopes), it has been found that in both types of HPV the proteins have approximately the same location and size of linear antigenic determinants; the difference is observed only in the form of small shifts in the size of several amino acid residues. However, there are some differences in the amino acid composition of epitopes; therefore, the possibility for cross-interaction of the antibodies with the antigens due to the similarity of linear antigenic determinants for B-cells is very small. The analysis of potential threedimensional epitopes for B-cells has shown that due to little difference between them the HPV16 L1 and HPV6 L1 proteins have no prerequisites for cross-interaction of the antibodies with the antigens belonging to the two different pathogenic HPV types. The analysis of probable linear epitopes for T-cells has revealed a common antigenic determinant in the two protein sequences. According to the rank made with the SYFPEITHI program, the amino acid sequence AQL(I)FNKPYWL is the second most likely antigenic determinant for T-cells. Meanwhile, the amino acid sequences of this determinant in HPV16 L1 and HPV6 L1 are virtually identical. There is a difference in only one position, but it is not critical due to the similarity of the physicochemical properties of amino acids, for which there is a replacement in the amino acid sequence of antigenic determinants. Consequently, some moderate cross-interaction of the antibodies to HPV16 L1 with the antigens of HPV6 L1 may be expected.

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4

Patanjali, S. R., S. U. Sajjan, and A. Surolia. "Erythrocyte-binding studies on an acidic lectin from winged bean (Psophocarpus tetragonolobus)." Biochemical Journal 252, no. 3 (June 15, 1988): 625–31. http://dx.doi.org/10.1042/bj2520625.

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An acidic lectin (WBA II) was isolated to homogeneity from the crude seed extract of the winged bean (Psophocarpus tetragonolobus) by affinity chromatography on lactosylaminoethyl-Bio-Gel. Binding of WBA II to human erythrocytes of type-A, -B and -O blood groups showed the presence of 10(5) receptors/cell, with high association constants (10(6)-10(8) M-1). Competitive binding studies with blood-group-specific lectins reveal that WBA II binds to H- and T-antigenic determinants on human erythrocytes. Affinity-chromatographic studies using A-, B-, H- and T-antigenic determinants coupled to an insoluble matrix confirm the specificity of WBA II towards H- and T-antigenic determinants. Inhibition of the binding of WBA II by various sugars show that N-acetylgalactosamine and T-antigenic disaccharide (Thomsen-Friedenreich antigen, Gal beta 1-3GalNAc) are the most potent mono- and di-saccharide inhibitors respectively. In addition, inhibition of the binding of WBA II to erythrocytes by dog intestine H-fucolipid prove that the lectin binds to H-antigenic determinant.

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5

Forsyth, IA, A. Hutchings, and GW Butcher. "A panel of monoclonal antibodies to ovine placental lactogen." Journal of Endocrinology 165, no. 2 (May 1, 2000): 435–42. http://dx.doi.org/10.1677/joe.0.1650435.

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A panel of 11 rat monoclonal antibodies (mAbs) has been raised to ovine placental lactogen (PL). By competitive enzyme-linked immunoabsorbent assay (ELISA), confirmed by two-site ELISA, the antibodies were shown to recognize six antigenic determinants on the ovine PL molecule, two of which overlap. One antigenic determinant (designated 1) was shared by other members of the prolactin/growth hormone (GH)/PL family in ruminants, humans and rodents. The binding of (125)I-labelled ovine PL to crude receptor preparations from sheep liver (somatotrophic) or rabbit mammary gland (lactogenic) was inhibited by mAbs recognizing antigenic determinants 2-6. Both types of receptor preparation were affected similarly. In the local in vivo pigeon crop sac assay, mAbs directed against determinants 3 and 6 enhanced the biological activity of ovine PL.

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6

Wetzler, Meir, M. T. Brady, S. N. J. Siat, S. Kakati, A. W. Block, X. Wang, S. P. Hunger, A. J. Carroll, and S. Ferrone. "Differential Antigenic Profile of High Molecular Weight-Melanoma Associated Antigen (HMW-MAA) Expressed by 11q23-Positive Acute Leukemia: An Immunotherapeutic Target." Blood 106, no. 11 (November 16, 2005): 3261. http://dx.doi.org/10.1182/blood.v106.11.3261.3261.

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Abstract The poor clinical response of 11q23-positive [also known as mixed lineage leukemia (MLL)] acute leukemia (AL) to chemotherapy-containing regimens has stimulated interest in developing alternative therapeutic strategies. Among them is immunotherapy. Since no leukemia-specific antigen has been identified in 11q23-positive AL, we are developing an antibody-based immunotherapeutic strategy which targets the HMW-MAA. This antigen, which is a membrane bound proteoglycan, represents an attractive target because of its high expression on the surface of 11q23-positive AL blasts and its restricted distribution in normal tissues. Taking advantage of a unique panel of monoclonal antibodies (mAb) recognizing 7 distinct and spatially distant antigenic determinants, we have analyzed the antigenic profile of HMW-MAA by flow cytometry in samples from 15 adult and 14 pediatric patients with 11q23-positive AL. Our results demonstrate a differential expression of the HMW-MAA antigenic determinants and that their expression pattern correlates with cytogenetic subgroups. Specifically, all the determinants were expressed on 6 adult samples [3 t(11;19)(q23;p13), 2 t(4;11)(q21;q23), and 1 t(10;11)(p12;q23)]. In contrast only 3 determinants were detected on 8 adult samples [3 t(9;11)(p22;q23), and 1 each with t(6;11)(q27;q23), t(11;12)(q23;q13), t(11;14)(q23;p11.2), inv(11)(q21q23.2) and add(11)(q23)]. No antigenic determinant was detected on leukemic cells from the adult patient with t(2;11)(p21;q23). Interestingly, the antigenic profile of HMW-MAA expressed on leukemic cells from pediatric patients was different, since all the determinants were expressed on leukemic cells from 6 t(4;11), 1 t(9;11), 1 t(11;1)(1;13;9)(q23;q25p34;q14.3;p13), 2 t(11;19) and 1 del(11)(q14q23). On the other hand no determinant was detectable on the leukemic cells from 3 children [1 with both t(1;11)(p32;q23) and t(4;11), 1 inv(11)(p15q23) and 1 add(11)(q23)]. Whether the difference in the antigenic profile of HMW-MAA expressed by adult and pediatric 11q23-positive AL cells reflects the different pathogenesis of AL in adults and children remains to be determined. Our data show that the differential expression of antigenic determinants of HMW-MAA on 11q23-positive AL cells does not reflect structural differences in the HMW-MAA expressed by various types of 11q23-positive AL as indicated by the results of Western blotting analysis. Further, the differential expression does not correlate with MLL gene rearrangement, since fluorescent in-situ hybridization (FISH) performed on 15 adult samples detected MLL gene rearrangement in 4 of the 6 samples that express all the determinants and in 6 of the 8 samples that express only 3 determinants. In addition, the pediatric sample with inv(11) that does not express any determinant, has MLL gene rearrangement by FISH. Finally, the differential expression does not correlate with the presence of MLL partial tandem duplication, since it was detected in 1 sample that expresses all the antigenic determinants and in 2 samples that express only 3 determinants. These findings emphasize the need to use more than one HMW-MAA-specific mAb to phenotype 11q23-positive AL and to select patients to be treated with HMW-MAA-specific antibody-based immunotherapy.

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7

Maeland, Johan A., Lars Bevanger, and Randi Valsoe Lyng. "Antigenic Determinants of Alpha-Like Proteins of Streptococcus agalactiae." Clinical Diagnostic Laboratory Immunology 11, no. 6 (November 2004): 1035–39. http://dx.doi.org/10.1128/cdli.11.6.1035-1039.2004.

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ABSTRACT The majority of group B streptococcus (GBS) isolates express one or more of a family of surface-anchored proteins that vary by strain and that form ladder-like patterns on Western blotting due to large repeat units. These proteins, which are important as GBS serotype markers and as inducers of protective antibodies, include the alpha C (Cα) and R4 proteins and the recently described alpha-like protein 2 (Alp2), encoded by alp2, and Alp3, encoded by alp3. In this study, we examined antigenic determinants possessed by Alp2 and Alp3 by testing of antibodies raised in rabbits, mainly by using enzyme-linked immunosorbent assays (ELISA) and an ELISA absorption test. The results showed that Alp2 and Alp3 shared an antigenic determinant, which may be a unique immunological marker of the Alp variants of GBS proteins. Alp2, in addition, possessed an antigenic determinant which showed specificity for Alp2 and a third determinant which showed serological cross-reactivity with Cα. Alp3, in addition to the determinant common to Alp2 and Alp3, harbored an antigenic site which also was present in the R4 protein, whereas no Alp3-specific antigenic site was detected. These ELISA-based results were confirmed by Western blotting and a fluorescent-antibody test. The results are consistent with highly complex antigenic structures of the alpha-like proteins in a fashion which is in agreement with the recently described structural mosaicism of the alp2 and alp3 genes. The results are expected to influence GBS serotyping, immunoprotection studies, and GBS vaccine developments.

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8

Pollard, K. Michael, and Michael G. Cohen. "Predicting Antigenic Determinants of Autoantigens." Autoimmunity 5, no. 4 (January 1990): 265–75. http://dx.doi.org/10.3109/08916939009014711.

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9

Rearden, A. "Evolution of glycophorin A in the hominoid primates studied with monoclonal antibodies, and description of a sialoglycoprotein analogous to human glycophorin B in chimpanzee." Journal of Immunology 136, no. 7 (April 1, 1986): 2504–9. http://dx.doi.org/10.4049/jimmunol.136.7.2504.

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Abstract Comparison of human and primate erythrocyte membrane sialoglycoproteins showed that common chimpanzee, dwarf chimpanzee, gorilla, orangutan, and gibbon have major periodic acid Schiff-positive proteins resembling human glycophorin A (GPA) monomer and dimer in electrophoretic mobility on sodium dodecyl sulfate-polyacrylamide gels. Immunoperoxidase staining of Western blots with monoclonal antibodies to human GPA showed that these primate bands express some GPA antigenic determinants. A new sialoglycoprotein analogous to human glycophorin B (GPB) was detected in common chimpanzee. Although human MN blood group phenotype results from an amino acid polymorphism of GPA, Western blots showed that in chimpanzee sialoglycoprotein (GPAch) always expresses the M blood group, whereas chimpanzee sialoglycoprotein (GPBch) expresses either the N blood group or a null phenotype. This result explains the detection of M and MN, but not of N, blood group phenotypes in chimpanzee. GPBch has higher apparent m.w. than human GPB, is present in the erythrocyte membrane in greater quantity than human GPB, and contains trypsin cleavage site(s) and the 10F7 determinant (both found on human GPA but not GPB). Expression of human GPA antigenic determinants was consistent with the phylogeny of the hominoid primates; common and dwarf chimpanzee expressed most of the determinants tested, gorilla and orangutan an intermediate number, and gibbon and siamang the least. Of the GPA antigenic determinants examined, the MN blood group determinants were most consistently expressed during evolution of the hominoid primates. The results suggested that variability in expression of GPA antigenic determinants between species was due to both differences in amino acid sequence and glycosylation.

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10

Zhang, Hong, Guangwen Wang, Jian Li, Yuchun Nie, Xuanling Shi, Gewei Lian, Wei Wang, et al. "Identification of an Antigenic Determinant on the S2 Domain of the Severe Acute Respiratory Syndrome Coronavirus Spike Glycoprotein Capable of Inducing Neutralizing Antibodies." Journal of Virology 78, no. 13 (July 1, 2004): 6938–45. http://dx.doi.org/10.1128/jvi.78.13.6938-6945.2004.

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ABSTRACT Severe acute respiratory syndrome (SARS) is a life-threatening disease caused by a newly identified coronavirus (CoV), SARS-CoV. The spike (S) glycoprotein of CoV is the major structural protein responsible for induction of host immune response and virus neutralization by antibodies. Hence, knowledge of neutralization determinants on the S protein is helpful for designing protective vaccines. To analyze the antigenic structure of the SARS-CoV S2 domain, the carboxyl-terminal half of the S protein, we first used sera from convalescent SARS patients to test the antigenicity of 12 overlapping fragments spanning the entire S2 and identified two antigenic determinants (Leu 803 to Ala 828 and Pro 1061 to Ser 1093). To determine whether neutralizing antibodies can be elicited by these two determinants, we immunized animals and found that both of them could induce the S2-specific antisera. In some animals, however, only one determinant (Leu 803 to Ala 828) was able to induce the antisera with the binding ability to the native S protein and the neutralizing activity to the SARS-CoV pseudovirus. This determinant is highly conserved across different SARS-CoV isolates. Identification of a conserved antigenic determinant on the S2 domain of the SARS-CoV S protein, which has the potential for inducing neutralizing antibodies, has implications in the development of effective vaccines against SARS-CoV.

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11

Jameson, B. A., and H. Wolf. "The antigenic index: a novel algorithm for predicting antigenic determinants." Bioinformatics 4, no. 1 (1988): 181–86. http://dx.doi.org/10.1093/bioinformatics/4.1.181.

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12

Feizi, T., and R. A. Childs. "Carbohydrates as antigenic determinants of glycoproteins." Biochemical Journal 245, no. 1 (July 1, 1987): 1–11. http://dx.doi.org/10.1042/bj2450001.

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13

Lynch, Dona M., and Stephen E. Howe. "Antigenic determinants in idiopathic thrombocytopenic purpura." British Journal of Haematology 63, no. 2 (March 12, 2008): 301–8. http://dx.doi.org/10.1111/j.1365-2141.1986.tb05553.x.

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14

Ametani, A., R. Apple, V. Bhardwaj, G. Gammon, A. Miller, and E. Sercarz. "Examining the Crypticity of Antigenic Determinants." Cold Spring Harbor Symposia on Quantitative Biology 54 (January 1, 1989): 505–11. http://dx.doi.org/10.1101/sqb.1989.054.01.060.

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15

Barlow, D. J., M. S. Edwards, and J. M. Thornton. "Continuous and discontinuous protein antigenic determinants." Nature 322, no. 6081 (August 1986): 747–48. http://dx.doi.org/10.1038/322747a0.

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16

Mehra, V., D. Sweetser, and R. A. Young. "Efficient mapping of protein antigenic determinants." Proceedings of the National Academy of Sciences 83, no. 18 (September 1, 1986): 7013–17. http://dx.doi.org/10.1073/pnas.83.18.7013.

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17

Beretta, Barbara, Amedeo Conti, Alessandro Fiocchi, Antonella Gaiaschi, Corrado L. Galli, Maria Gabriella Giuffrida, Cinzia Ballabio, and Patrizia Restani. "Antigenic Determinants of Bovine Serum Albumin." International Archives of Allergy and Immunology 126, no. 3 (2001): 188–95. http://dx.doi.org/10.1159/000049513.

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18

Elsayed, S., A. S. E. Hammer, M. B. Kalvenes, E. Florvaag, J. Apold, and H. Vik. "Antigenic and Allergenic Determinants of Ovalbumin." International Archives of Allergy and Immunology 79, no. 1 (1986): 101–6. http://dx.doi.org/10.1159/000233952.

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19

ELSAYED, S., E. HOLEN, and M. B. HAUGSTAD. "Antigenic and Allergenic Determinants of Ovalbumin." Scandinavian Journal of Immunology 27, no. 5 (May 1988): 587–91. http://dx.doi.org/10.1111/j.1365-3083.1988.tb02386.x.

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20

Geysen, H. Mario, Tom J. Mason, and Stuart J. Rodda. "Cognitive features of continuous antigenic determinants." Journal of Molecular Recognition 1, no. 1 (February 1988): 32–41. http://dx.doi.org/10.1002/jmr.300010107.

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21

Geysen, H. M., T. J. Mason, and S. J. Rodda. "Cognitive features of continuous antigenic determinants." Journal of Molecular Recognition 2, no. 1 (July 1989): 49. http://dx.doi.org/10.1002/jmr.300020108.

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22

Murdin, A. D., H. h. Lu, M. G. Murray, and E. Wimmer. "Poliovirus antigenic hybrids simultaneously expressing antigenic determinants from all three serotypes." Journal of General Virology 73, no. 3 (March 1, 1992): 607–11. http://dx.doi.org/10.1099/0022-1317-73-3-607.

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23

Yuexi, Li, Wang Xingsheng, Liao Jianmin, Yin Dengke, Li Suqin, Wang Zhengmao, Li Lin, and Xie Guangyan. "Computer analysis and identification of antigenic determinants from five glycoproteins of HSV2 (155.17)." Journal of Immunology 186, no. 1_Supplement (April 1, 2011): 155.17. http://dx.doi.org/10.4049/jimmunol.186.supp.155.17.

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Abstract To screen the antigenic determinants from glycoprotein B (gB2), C (gC2), E (gE2), G (gG2) and I (gI2) of herpes simplex virus II (HSV2) for designing novel vaacine, the aminao acid sequences of the five proteins were analysed with several software algorithms, DNAstar, Biosun, and Antheprot. The common antigenic determinants screened by all the software algorithms were synthesized chenically and identified by animal immune experiments. Sixteen synthesized antigenic determinants selected from the five proteins were linked to carrier protein BSA respectively to enhance their immunogenicity, and uesed as immunogens to immunize mice. The antibodies in the sera of the immunized mice were detected with the coreesponding immunogens and the parent glycoproteins by EIA and western blotting. The virus-neutralizing activity of the antisera were tested with vero cell in vitro. The antisera reacted strongly with the parent glycoproteins, and also the peptides reacted strongly with antibodies against the parent glycoproteins. The antisera against five antigenic determinants from gB2 ,gC2, gE2, gG2, and gI2 can neutralize HSV2 infectivity in vitro respectively, which has not been reported up to now. These results suggested that the antigenic determinants from the five glycoproteins screened by software algorithms and validated by experiments are promising for vaccine design.

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Maeland, Johan A., Lars Bevanger, and Randi Valsoe Lyng. "Immunological Markers of the R4 Protein of Streptococcus agalactiae." Clinical Diagnostic Laboratory Immunology 12, no. 11 (November 2005): 1305–10. http://dx.doi.org/10.1128/cdli.12.11.1305-1310.2005.

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ABSTRACT This study focuses on immunological markers of R4, an important Streptococcus group B (GBS) protein. The results obtained by using rabbit antisera and purified proteins for antigens in enzyme-linked immunosorbent assay-based experiments provided evidence that R4 possesses two antigenic determinants. One of the determinants is shared with the alpha-like protein 3 (Alp3) of GBS, was named R4/Alp3 common, and was expressed by GBS, which possessed the Alp3-encoding gene alp3 or the R4-encoding gene rib. The other antigenic determinant was detected only in rib-positive GBS organisms and was named R4 specific. This determinant probably is an immunological marker unique to the R4 protein. Neither of the antigenic R4 determinants showed serological cross-reactivity with the GBS proteins Cα, Cβ, and R3 or with alpha-like protein 2. Of 60 clinical serotype III GBS strains, 56 (93%) isolates possessed the rib gene and 50 (89%) of the rib-positive isolates expressed levels of R4 detectable by antibody-based tests, consistent with R4 expression failure or low-level expression in ∼10% of rib-positive GBS. alp3 was not detected in type III GBS but was possessed by six of eight type V strains and six of six type VIII strains. All alp3-positive strains were recognized by the R4/Alp3 common antibodies, but none of them were recognized by the R4-specific antibodies. NCTC 9828, a reference strain for R3 and R4, expressed the determinant R4/Alp3 common but not R4 specific. A monoclonal R4 antibody, previously considered to be R4 specific and used in GBS serotyping, targeted R4/Alp3 common and is thus not R4 specific. The results show that failure to discriminate between R4 specific and R4/Alp3 common by antisera designed for GBS serotyping can result in the false identification of Alp3 as R4 or vice versa, whereas anti-R4 antibodies targeting only the determinant R4 specific will detect only R4. Both R4 and Alp3 need further evaluation with respect to the immunobiological function of each distinct antigenic determinant, for instance, with regard to their potential as GBS vaccine components.

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25

Filex Otieno and Michael Walekhwa. "COVID-19 Vaccines Confer a Prophylactic Effect on Common Cold." Kabarak Journal of Research & Innovation 11, no. 3 (November 14, 2021): 251–56. http://dx.doi.org/10.58216/kjri.v11i3.76.

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Common cold is an upper respiratory infection with relatively high mortality and infection rate. This is especially true among immunosuppressed individuals. The infection can be caused by human coronaviruses of which common cold coronaviruses-229E, -NL63, -OC43, and -HKU1 are the major etiological agents. These viruses also belong to the same family as the SARS-CoV-2 virus that cause the COVID-19 pandemic. The pandemic has led to the development of the various COVID-19 vaccines. The coronaviruses all express similar types of proteins, the membrane, spike, envelope protein, and the nucleocapsid. The spike protein is the main antigenic determinant and also induces an endoplasmic reticulum stress response. Cross-reactivity on the antigenic determinants between both groups of coronaviruses exists due to similar main antigenic orientation. Studies on the strength of the immune responses evoked by either SARS-CoV-2 or the human common cold coronaviruses towards each other is inconclusive; averagely demonstrating that antibodies (Abs) against SARS-CoV-2 can neutralize antigens (Ags) on common cold coronaviruses. Due to cross-reactivity, theoretically vaccines against SARS-CoV-2 can be used to fight common cold coronavirus infections due to the two expressing similar antigenic determinants that elicit an immune response for the homologous antigen.

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Nobile-Orazio, Eduardo. "Antigenic Determinants in IgM Paraprotein-Related Neuropathies." Clinical Lymphoma and Myeloma 9, no. 1 (March 2009): 107–9. http://dx.doi.org/10.3816/clm.2009.n.029.

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27

Wood, John N., Nicholas B. Lathangue, Donald R. McLachlan, Bryan J. Smith, Brian H. Anderton, and Alan J. Dowding. "Chromatin Proteins Share Antigenic Determinants with Neurofilaments." Journal of Neurochemistry 44, no. 1 (January 1985): 149–54. http://dx.doi.org/10.1111/j.1471-4159.1985.tb07124.x.

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Cao, Sam Linsen, Ann Progulske-Fox, Jeffrey D. Hillman, and Martin Handfield. "In vivo induced antigenic determinants ofActinobacillus actinomycetemcomitans." FEMS Microbiology Letters 237, no. 1 (August 2004): 97–103. http://dx.doi.org/10.1111/j.1574-6968.2004.tb09683.x.

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29

Richiardi, P., T. Crepaldi, F. Malavasi, E. Olivetti, and A. O. Carbonara. "Further antigenic determinants on HLA-A molecules." Tissue Antigens 25, no. 2 (December 11, 2008): 69–74. http://dx.doi.org/10.1111/j.1399-0039.1985.tb00416.x.

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30

Hinz, K. H. "Heat-stable Antigenic Determinants of Haemophilus paragallinarum." Zentralblatt für Veterinärmedizin Reihe B 27, no. 8 (May 13, 2010): 668–76. http://dx.doi.org/10.1111/j.1439-0450.1980.tb01730.x.

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31

Blaas-Mautner, P., S. Filsinger, B. Berger, D. Roelcke, and G. M. Hänsch. "C8 binding protein bears I antigenic determinants." Annals of Hematology 62, no. 2-3 (February 1991): 64–67. http://dx.doi.org/10.1007/bf01714902.

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32

Scott, M. D., K. L. Murad, F. Koumpouras, M. Talbot, and J. W. Eaton. "Chemical camouflage of antigenic determinants: Stealth erythrocytes." Proceedings of the National Academy of Sciences 94, no. 14 (July 8, 1997): 7566–71. http://dx.doi.org/10.1073/pnas.94.14.7566.

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Marcel, Y. L., T. L. Innerarity, C. Spilman, R. W. Mahley, A. A. Protter, and R. W. Milne. "Mapping of human apolipoprotein B antigenic determinants." Arteriosclerosis: An Official Journal of the American Heart Association, Inc. 7, no. 2 (March 1987): 166–75. http://dx.doi.org/10.1161/01.atv.7.2.166.

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Dotta, F., and U. Mario. "Antigenic determinants in type 1 diabetes mellitus:." APMIS 104, no. 7-8 (July 8, 1996): 769–74. http://dx.doi.org/10.1111/j.1699-0463.1996.tb04941.x.

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Kent, Karen A., and James Robinson. "Antigenic determinants on HIV-1 envelope glycoproteins." AIDS 10, Supplement (January 1996): S107–114. http://dx.doi.org/10.1097/00002030-199601001-00015.

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Werkmeister, J. A., and J. A. M. Ramshaw. "Multiple antigenic determinants on type III collagen." Biochemical Journal 274, no. 3 (March 15, 1991): 895–98. http://dx.doi.org/10.1042/bj2740895.

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Eight monoclonal antibodies have been produced against human pepsin-soluble type III collagen. All antibodies were shown to be highly specific for type III collagen and did not cross-react with a range of other collagen types or connective-tissue proteins. Examination of type III collagen from other species showed that these antibodies had a wide range of species specificities, indicating that several distinct epitopes were being recognized. The location of the epitopes was investigated by using reactivity of the antibodies to CNBr fragments and to sequential fragments formed by tryptic digestion of renaturing type III collagen. These data also indicated that several distinct epitopes were recognized and that they were located over the length of the type III collagen.

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BenEzra, D., and C. C. Chan. "S-100 antigenic determinants in human retina." Graefes Archive for Clinical and Experimental Ophthalmology 225, no. 2 (April 1987): 151–53. http://dx.doi.org/10.1007/bf02160349.

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Suzuki, G., and R. H. Schwartz. "The pigeon cytochrome c-specific T cell response of low responder mice. I. Identification of antigenic determinants on fragment 1 to 65." Journal of Immunology 136, no. 1 (January 1, 1986): 230–39. http://dx.doi.org/10.4049/jimmunol.136.1.230.

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Abstract An examination of the proliferative response to pigeon cytochrome c fragments 1 to 65 and 1 to 80 by T cells from mice that are low responders to the native molecule revealed that some of the strains could respond to antigenic determinants on these fragments. T cell clones derived from B10.A(3R) and B10.A(4R) mice were used to characterize the antigenic determinants on fragment 1 to 65. All of the clones recognized syngeneic A beta:A alpha Ia molecules as their restriction element. Three B10.A(3R) clones and six B10.A(4R) clones recognized fragment 39 to 65. Another four B10.A(4R) clones responded to fragment 1 to 38. By stimulating with a series of cytochrome c fragments from different species, as well as a synthetic peptide, it was possible to localize the antigenic determinant(s) recognized by the B10.A(3R) clones to residues 45 to 58. Each clone showed a unique pattern of responsiveness to the various fragments, suggesting a diversity of T cell receptors specific for the same peptide. One B10.A(3R) clone could be stimulated by many of the 1 to 65 fragments in association with allogeneic B10.SM presenting cells and by tuna fragment 1 to 65 in association with B10.M presenting cells, although the rank order of potency for several of the fragments was different than that observed with syngeneic antigen-presenting cells. In addition, the clone was poorly reactive to a synthetic peptide containing a conservative substitution, serine for threonine, at position 49. The implications of these results for subsite dissection (agretope and epitope) of the antigenic determinant recognized by this clone are discussed.

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Aldrich, C. J., R. N. Jenkins, and R. R. Rich. "Clonal analysis of the anti-Qa-1 cytotoxic T lymphocyte repertoire: definition of the Qa-1d and Qa-1c alloantigens and cross-reactivity with H-2." Journal of Immunology 136, no. 2 (January 15, 1986): 383–88. http://dx.doi.org/10.4049/jimmunol.136.2.383.

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Abstract To characterize the four common Qa-1 allelic products, we examined in detail the CTL-defined determinants encoded by Qa-1. In previous studies with anti-Qa-1 CTL and alloantisera, investigators have described antigenic determinants present on Qa-1a and Qa-1b antigens, but they have defined Qa-1c and Qa-1d exclusively by their cross-reactivity with Qa-1a and/or Qa-1b determinants. To delineate further the CTL-defined determinants encoded by Qa-1d, we generated CTL clones with Qa-1d specificity and demonstrated that the Qa-1d molecule expressed determinants that were not detected on Qa-1a, Qa-1b, or Qa-1c target cells. Other CTL clones derived from anti-Qa-1d MLC recognized new antigenic determinants on Qa-1c that cross-reacted with Qa-1d. Each of the four common Qa-1 phenotypes was shown to exhibit unique antigenic determinants. In addition, Qa-1d anti-Qa-1a and Qa-1d anti-Qa-1b CTL confirmed extensive cross-reactivity among these Qa-1 alloantigens. Analysis of CTL from these four immunizations also resulted in the isolation of Qa-1a-specific and Qa-1d-specific CTL clones that cross-reacted with H-2Df and H-2Ks, respectively.

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Robert, Francoise M., and E. L. Schmidt. "Somatic serogroups among 55 strains of Rhizobium phaseoli." Canadian Journal of Microbiology 31, no. 6 (June 1, 1985): 519–23. http://dx.doi.org/10.1139/m85-097.

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The serological relationships among 55 strains of Rhizobium phaseoli of diverse geographical origin were examined by direct immunofluorescence. Five clear-cut serogroups and a minimum of 11 somatic antigenic determinants were detected among 42 strains using 11 fluorescent antibodies. At least a sixth serogroup exists to account for the remaining 13 unreactive strains. Serogroups 1 and 2 comprised a large number of strains (15 and 21, respectively), whereas serogroup 3 comprised only 4 strains and serogroups 4 and 5 a single strain each. These findings attest to a high degree of antigenic diversity as well as a high incidence of certain antigenic determinants in the collection of R. phaseoli examined. As a consequence, choice candidates for ecological studies would be strains endowed with a distinctive antigenic make-up as in serogroups 4 and 5.

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Huang, Sheng-Wen, Ching-Hui Tai, Judith M. Fonville, Chin-Hui Lin, Shih-Min Wang, Ching-Chung Liu, Ih-Jen Su, Derek J. Smith, and Jen-Ren Wang. "Mapping Enterovirus A71 Antigenic Determinants from Viral Evolution." Journal of Virology 89, no. 22 (September 2, 2015): 11500–11506. http://dx.doi.org/10.1128/jvi.02035-15.

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ABSTRACTHuman enterovirus A71 (EV-A71) belongs to theEnterovirus Aspecies in thePicornaviridaefamily. Several vaccines against EV-A71, a disease causing severe neurological complications or even death, are currently under development and being tested in clinical trials, and preventative vaccination programs are expected to start soon. To characterize the potential for antigenic change of EV-A71, we compared the sequences of two antigenically diverse genotype B4 and B5 strains of EV-A71 and identified substitutions at residues 98, 145, and 164 in the VP1 capsid protein as antigenic determinants. To examine the effects of these three substitutions on antigenicity, we constructed a series of recombinant viruses containing different mutation combinations at these three residues with a reverse genetics system and then investigated the molecular basis of antigenic changes with antigenic cartography. We found that a novel EV-A71 mutant, containing lysine, glutamine, and glutamic acid at the respective residues 98, 145, and 164 in the VP1 capsid protein, exhibited neutralization reduction against patients' antisera and substantially increased virus binding ability to human cells. These observations indicated that this low-neutralization-reactive EV-A71 VP1-98K/145Q/164E mutant potentially increases viral binding ability and that surveillance studies should look out for these mutants, which could compromise vaccine efficacy.IMPORTANCEEmerging and reemerging EV-A71 viruses can cause severe neurological etiology, primarily affecting children, especially around Asia-Pacific countries. We identified a set of mutations in EV-A71 that both reduced neutralization activity against humoral immunity in antisera of patients and healthy adults and greatly increased the viral binding ability to cells. These findings provide important insights for EV-A71 antigenic determinants and emphasize the importance of continuous surveillance, especially after EV-A71 vaccination programs begin.

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Fu, Tong-Ming, Lawrence M. Mylin, Todd D. Schell, Igor Bacik, Gustav Russ, Jonathan W. Yewdell, Jack R. Bennink, and Satvir S. Tevethia. "An Endoplasmic Reticulum-Targeting Signal Sequence Enhances the Immunogenicity of an Immunorecessive Simian Virus 40 Large T Antigen Cytotoxic T-Lymphocyte Epitope." Journal of Virology 72, no. 2 (February 1, 1998): 1469–81. http://dx.doi.org/10.1128/jvi.72.2.1469-1481.1998.

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ABSTRACT An immunological hierarchy among three H-2Db-restricted cytotoxic T lymphocyte (CTL) determinants in simian virus 40 (SV40) large T antigen (Tag) was described previously: determinants I and II/III are immunodominant, whereas determinant V is immunorecessive. To assess the immunogenicity of each determinant individually and define mechanisms that contribute to the immunorecessive nature of determinant V, we constructed a panel of recombinant vaccinia viruses (rVVs) expressing minigenes encoding these determinants in various polypeptide contexts. We found the following. (i) Immunization of mice with an rVV encoding full-length SV40 Tag resulted in priming for CTL responses to determinants I and II/III but not determinant V. (ii) rVVs encoding peptide I or II/III in the cytosol or targeted to the endoplasmic reticulum (ER) were highly antigenic and immunogenic. (iii) rVVs encoding peptide V minigenes were antigenic and immunogenic if the peptide was targeted to the ER, expressed in the cytosol with short flanking sequences, or expressed from within a self-protein, murine dihydrofolate reductase. (iv) Presentation of the nonflanked peptide V (preceded by a Met codon only) could be enhanced by using a potent inhibitor of the proteasome. (v) H-2Db–epitope V peptide complexes decayed more rapidly than complexes containing epitope I or II/III peptides. In brefeldin A blocking experiments, functional epitope V complexes were detected longer on targets expressing ER-targeted epitope V than on targets expressing forms of epitope V dependent on the transporter associated with antigen processing. Therefore, limited formation of relatively unstable cell surface H-2Db complexes most likely contributes to the immunorecessive nature of epitope V within SV40 Tag. Increasing the delivery of epitope V peptide to the major histocompatibility complex class I presentation pathway by ER targeting dramatically enhanced the immunogenicity of epitope V.

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Kendra, Joseph A., Kentaro Tohma, Lauren A. Ford-Siltz, Cara J. Lepore, and Gabriel I. Parra. "Antigenic cartography reveals complexities of genetic determinants that lead to antigenic differences among pandemic GII.4 noroviruses." Proceedings of the National Academy of Sciences 118, no. 11 (March 8, 2021): e2015874118. http://dx.doi.org/10.1073/pnas.2015874118.

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Noroviruses are the predominant cause of acute gastroenteritis, with a single genotype (GII.4) responsible for the majority of infections. This prevalence is characterized by the periodic emergence of new variants that present substitutions at antigenic sites of the major structural protein (VP1), facilitating escape from herd immunity. Notably, the contribution of intravariant mutations to changes in antigenic properties is unknown. We performed a comprehensive antigenic analysis on a virus-like particle panel representing major chronological GII.4 variants to investigate diversification at the inter- and intravariant level. Immunoassays, neutralization data, and cartography analyses showed antigenic similarities between phylogenetically related variants, with major switches to antigenic properties observed over the evolution of GII.4 variants. Genetic analysis indicated that multiple coevolving amino acid changes—primarily at antigenic sites—are associated with the antigenic diversification of GII.4 variants. These data highlight complexities of the genetic determinants and provide a framework for the antigenic characterization of emerging GII.4 noroviruses.

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Kvam, Augusta I., Rooyen T. Mavenyengwa, Andreas Radtke, and Johan A. Maeland. "Streptococcus agalactiae Alpha-Like Protein 1 Possesses Both Cross-Reacting and Alp1-Specific Epitopes." Clinical and Vaccine Immunology 18, no. 8 (June 8, 2011): 1365–70. http://dx.doi.org/10.1128/cvi.05005-11.

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ABSTRACTMost isolates of group B streptococci (GBS) express an alpha-like protein (Alp), Cα (encoded bybca), Alp1 (also called epsilon;alp1), Alp2 (alp2), Alp3 (alp3), Alp4 (alp4), or R4/Rib (rib). These proteins are chimeras with a mosaic structure and with antigenic determinants with variable immunological cross-reactivities between the Alps, including Alp1 and Cα cross-reactivity. This study focused on antigenic domains of Alp1, studied by using rabbit antisera in immunofluorescence, Western blotting, and enzyme-linked immunosorbent assay (ELISA)-based tests and whole cells of GBS or trypsin-extracted and partially purified antigens from the strains A909 (serotype Ia/Cα, Cβ) and 335 (Ia/Alp1). Alp1 and Cα shared an antigenic determinant, Alp1/Cα common, not harbored by other Alps, probably located in the Alp1 and Cα repeat units, as these units are nearly identical in genomic sequence. An antigenic Alp1 determinant was Alp1 specific and was most likely located in the N-terminal unit of Alp1 in which an Alp1-specific primer site for PCR is also located. In addition, Alp1 possessed a domain with low immunogenicity which cross-reacted immunologically with Alp2 and Alp3, with unknown location in Alp1. Alp1 was partially degraded by trypsin during antigen extraction but with the antigenic domains preserved. The results indicate that Cα and Alp1 are immunologically related in the same manner that R4 (Rib) and Alp3 are related. The domain called Alp1 specific should be important in GBS serotyping as a surface-anchored serosubtype marker. The Alp1/Cα common determinant may be of prime interest as an immunogenic domain in a GBS vaccine.

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Gould, K. G., H. Scotney, A. R. Townsend, J. Bastin, and G. G. Brownlee. "Mouse H-2k-restricted cytotoxic T cells recognize antigenic determinants in both the HA1 and HA2 subunits of the influenza A/PR/8/34 hemagglutinin." Journal of Experimental Medicine 166, no. 3 (September 1, 1987): 693–701. http://dx.doi.org/10.1084/jem.166.3.693.

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We have constructed two chimeric influenza hemagglutinin (HA) genes in which the HA1 and HA2 subunits of the HA molecule have been interchanged between influenza A/PR/8/34 (H1 subtype) and A/NT/60/68 (H3 subtype). These genes were used to construct recombinant vaccinia viruses that expressed intact chimeric HA. These recombinant viruses were used to test whether murine CTL recognize antigenic determinants in either the HA1, HA2, or both subunits. We found that both subunits of the HA molecule contain determinants for CTL. This implies that CTL have, at least in part, separate antigenic determinants from B lymphocytes, which recognize mainly epitopes within the HA1 subunit.

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Chowdhury, Fatema Moni, Sirajul Islam Khan, Nils Kåre Birkeland, and Chowdhury Rafiqul Ahsan. "Antigenic Cross-Reactivity Between Escherichia albertii DM104 and Different Shigella spp." Bangladesh Journal of Microbiology 35, no. 1 (January 15, 2019): 17–21. http://dx.doi.org/10.3329/bjm.v35i1.39799.

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Environmental Escherichia albertii strain DM104 has been found to induce protective immunity against Shigella dysenteriae in guinea pig model and intranasal immunization showed promising results in terms of antibody response and protective efficacy. For selecting a proper immunodiagnostics marker against shigellosis, the current study investigated the antigenic cross-reactivity between DM104 and four different Shigella spp (S. dysenteriae type 4, S. flexneri type 2a, S. boydii type 15 and S. sonnei). At least six antigenic protein bands (85, 72, 34, 30, 23 and 20 k Da) of the surface components from all these species reacted strongly with both homologous and heterologous antisera, suggesting common distribution of antigenic determinants/epitopes in these bacterial species. This experiment, thus gave a clear idea of the level of antigenic determinants/epitopes sharing and variations between the DM104 and four Shigella spp. Results from this study suggest that the 34, 23 and 20 k Da antigenic proteins may be incorporated as immunodiagnostic marker for the detection of different Shigella spp. Bangladesh J Microbiol, Volume 35 Number 1 June 2018, pp 17-21

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ARAI, Kayoko, Junichi YASUDA, Takako SASAKI, and Kunio YONEMASU. "ANTIGENIC DETERMINANTS RESULTING FROM POLYMERIZATION OF IMMUNOGLOBULIN G." Japanese Journal of Medical Science and Biology 41, no. 5-6 (1988): 189–96. http://dx.doi.org/10.7883/yoken1952.41.189.

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Alves, Leila Lopes, Luiz R. Travassos, José O. Previato, and Lúcia Mendonça-Previato. "Novel antigenic determinants from peptidorhamnomannans of Sporothrix schenckii." Glycobiology 4, no. 3 (June 1, 1994): 281–88. http://dx.doi.org/10.1093/glycob/4.3.281.

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SKAMNIOTI, PARASKEVI, and CHRISTOPHER J. RIDOUT. "Microbial avirulence determinants: guided missiles or antigenic flak?" Molecular Plant Pathology 6, no. 5 (September 2005): 551–59. http://dx.doi.org/10.1111/j.1364-3703.2005.00302.x.

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Finlay, B. B., L. S. Frost, W. Paranchych, J. M. Parker, and R. S. Hodges. "Major antigenic determinants of F and ColB2 pili." Journal of Bacteriology 163, no. 1 (1985): 331–35. http://dx.doi.org/10.1128/jb.163.1.331-335.1985.

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