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Journal articles on the topic 'Cross-species reactivity'

Author: Grafiati

Published: 7 July 2024

Last updated: 31 July 2025

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1

ARLIAN, L., C. RAPP, and E. FERNANDEZCALDAS. "Allergenicity of and its cross-reactivity with species." Journal of Allergy and Clinical Immunology 91, no. 5 (1993): 1051–58. http://dx.doi.org/10.1016/0091-6749(93)90219-6.

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RESTANI, GAIASCHI, PLEBANI, et al. "Cross-reactivity between milk proteins from different animal species." Clinical & Experimental Allergy 29, no. 7 (1999): 997–1004. http://dx.doi.org/10.1046/j.1365-2222.1999.00563.x.

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3

SU, JUI-LAN, STEVE STIMPSON, CHRISTINE EDWARDS, JOHN VAN ARNOLD, SUSAN BURGESS, and PEIYUAN LIN. "Neutralizing IGF-1 Monoclonal Antibody With Cross-Species Reactivity." Hybridoma 16, no. 6 (1997): 513–18. http://dx.doi.org/10.1089/hyb.1997.16.513.

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4

Christensen, L. H., C. Hejl, H. Henmar, N. Johansen, and H. Ipsen. "Extensive IgE Cross-reactivity towards Different US Ragweed Species." Journal of Allergy and Clinical Immunology 125, no. 2 (2010): AB17. http://dx.doi.org/10.1016/j.jaci.2009.12.098.

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5

Losada, S., N. Chacón, C.Colmenares, et al. "Schistosoma: Cross-reactivity and antigenic community among different species." Experimental Parasitology 111, no. 3 (2005): 182–90. http://dx.doi.org/10.1016/j.exppara.2005.07.007.

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Gersten, Douglas M., and Vincent J. Hearing. "Antigens of Murine Melanoma and Their Cross-Species Reactivity." Pathobiology 60, no. 1 (1992): 49–56. http://dx.doi.org/10.1159/000163697.

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7

Van den Bossche, D., A. De Bel, M. Hendrickx, et al. "Galactomannan Enzymatic Immunoassay Cross-Reactivity Caused by Prototheca Species." Journal of Clinical Microbiology 50, no. 10 (2012): 3371–73. http://dx.doi.org/10.1128/jcm.01028-12.

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Gupta, R., B. P. Singh, S. Sridhara, et al. "Allergenic cross-reactivity ofCurvularia lunatawith other airborne fungal species." Allergy 57, no. 7 (2002): 636–40. http://dx.doi.org/10.1034/j.1398-9995.2002.03331.x.

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Conrad, Melanie L., William C. Davis, and Ben F. Koop. "TCR and CD3 antibody cross-reactivity in 44 species." Cytometry Part A 71A, no. 11 (2007): 925–33. http://dx.doi.org/10.1002/cyto.a.20435.

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10

Emiliani, Yuliana, Andrés Sánchez, Marlon Munera, Jorge Sánchez, and Dilia Aparicio. "In silico analysis of cross reactivity among phospholipases from Hymenoptera species." F1000Research 10 (March 29, 2021): 2. http://dx.doi.org/10.12688/f1000research.27089.2.

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Background: Phospholipases are enzymes with the capacity to hydrolyze membrane lipids and have been characterized in several allergenic sources, such as hymenoptera species. However, cross-reactivity among phospholipases allergens are little understood. The objective of this study was to determine potential antigenic regions involved in cross-reactivity among allergens of phospholipases using an in silico approach. Methods: In total, 18 amino acids sequences belonging to phospholipase family derived from species of the order hymenoptera were retrieved from the UniProt database to perform phylo

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Emiliani, Yuliana, Andrés Sánchez, Marlon Munera, Jorge Sánchez, and Dilia Aparicio. "In silico analysis of cross reactivity among phospholipases from Hymenoptera species." F1000Research 10 (January 5, 2021): 2. http://dx.doi.org/10.12688/f1000research.27089.1.

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Background: Phospholipases are enzymes with the capacity to hydrolyze membrane lipids and have been characterized in several allergenic sources, such as hymenoptera species. However, cross-reactivity among phospholipases allergens are little understood. The objective of this study was to determine potential antigenic regions involved in cross-reactivity among allergens of phospholipases using an in silico approach. Methods: In total, 18 amino acids sequences belonging to phospholipase family derived from species of the order hymenoptera were retrieved from the UniProt database to perform phylo

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12

Zhou, Wei, Kaylah Bias, Dylan Lenczewski-Jowers, et al. "Analysis of Protein Sequence Identity, Binding Sites, and 3D Structures Identifies Eight Pollen Species and Ten Fruit Species with High Risk of Cross-Reactive Allergies." Genes 13, no. 8 (2022): 1464. http://dx.doi.org/10.3390/genes13081464.

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Fruit allergens are proteins from fruits or pollen that cause allergy in humans, an increasing food safety concern worldwide. With the globalization of food trade and changing lifestyles and dietary habits, characterization and identification of these allergens are urgently needed to inform public awareness, diagnosis and treatment of allergies, drug design, as well as food standards and regulations. This study conducted a phylogenetic reconstruction and protein clustering among 60 fruit and pollen allergens from 19 species, and analyzed the clusters, in silico, for cross-reactivity (IgE), 3D

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13

Vordermeier, H. Martin, Jemma Brown, Paul J. Cockle, et al. "Assessment of Cross-Reactivity between Mycobacterium bovis and M. kansasii ESAT-6 and CFP-10 at the T-Cell Epitope Level." Clinical and Vaccine Immunology 14, no. 9 (2007): 1203–9. http://dx.doi.org/10.1128/cvi.00116-07.

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ABSTRACT Cross-reactivity between Mycobacterium kansasii ESAT-6 and CFP-10 homologues and their M. bovis counterparts can confound the interpretation of immunodiagnostic tests for tuberculosis. M. kansasii is a nontuberculous mycobacterial species cultured from skin test-positive cattle in Great Britain. Using peptides derived from M. bovis and M. kansasii ESAT-6 and CFP-10 regions that differ between these species, we investigated the species specificity and cross-reactivity at the level of individual bovine T-cell epitopes. Our results demonstrated that all peptides tested are fully cross-re

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14

Mummah, Riley O., Ana C. R. Gomez, Angela H. Guglielmino, et al. "Navigating cross-reactivity and host species effects in a serological assay: A case study of the microscopic agglutination test for Leptospira serology." PLOS Neglected Tropical Diseases 18, no. 10 (2024): e0012042. http://dx.doi.org/10.1371/journal.pntd.0012042.

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Background Serology (the detection of antibodies formed by the host against an infecting pathogen) is frequently used to assess current infections and past exposure to specific pathogens. However, the presence of cross-reactivity among host antibodies in serological data makes it challenging to interpret the patterns and draw reliable conclusions about the infecting pathogen or strain. Methodology/Principal findings In our study, we use microscopic agglutination test (MAT) serological data from three host species [California sea lion (Zalophus californianus), island fox (Urocyon littoralis), a

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15

Thomas, C. B., D. E. Jasper, J. T. Boothby, and J. D. Dellinger. "Enzyme-linked immunosorbent assay for detection of Mycoplasma californicum-specific antibody in bovine serum: Optimization of assay determinants and control of serologic cross-reactions." American Journal of Veterinary Research 48, no. 4 (1987): 590–95. https://doi.org/10.2460/ajvr.1987.48.04.590.

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SUMMARY An enzyme-linked immunosorbent assay (elisa) was adapted to detect Mycoplasma californicum-specific antibodies in bovine serum. Cross-reactive antibody was found in the M californicum-positive reference serum when assayed against each of 7 solid-phase antigens of heterologous mycoplasma species. Cross-reactivity was further demonstrated by inhibition of elisa reactivity to M californicum solid-phase antigen by incubation of sera with antigen suspensions of each heterologous species. Incubation of test sera with a cross-reacting antigen mixture containing equal proportions of the 7 cros

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16

Berger, Bradley J., and A. Rashid Bhatti. "Snake venom components and their cross-reactivity: a review." Biochemistry and Cell Biology 67, no. 9 (1989): 597–601. http://dx.doi.org/10.1139/o89-092.

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Snake venoms are complex mixtures of organic and inorganic compounds, many of which display biological activity. It has been demonstrated that antisera raised against whole venom or a single purified venom protein from one species of snake will react with proteins in the venom of other species. This cross-reactivity between species may have applications in determining snake phylogeny, but recent studies on the variation of venom components within a species make these evolutionary conclusions questionable.Key words: snake, venom, cross-reactive, evolution.

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17

Rizk, Raeda Z., Neil D. Christensen, Kristina M. Michael, et al. "Reactivity pattern of 92 monoclonal antibodies with 15 human papillomavirus types." Journal of General Virology 89, no. 1 (2008): 117–29. http://dx.doi.org/10.1099/vir.0.83145-0.

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Most anti-human papillomavirus (HPV) capsid antibody assays are based on virus-like particles (VLP). We evaluated glutathione S-transferase (GST)–L1 fusion proteins as ELISA antigens for determining type specificity and cross-reactivity of 92 VLP-specific monoclonal antibodies (mAb) generated against nine mucosal alpha papillomavirus types of species 7, 9 and 10. The antibody panel included 25 new mAb, and 24 previously published mAb are further characterized. We determined the cross-reactivity patterns with 15 different HPV types representing 6 species (alpha1, 2, 4, 7, 9 and 10) and neutrali

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18

Holm, Bettina E., Noreen Sandhu, Julie Tronstrøm, Magnus Lydolph, Nicole H. Trier, and Gunnar Houen. "Species cross-reactivity of rheumatoid factors and implications for immunoassays." Scandinavian Journal of Clinical and Laboratory Investigation 75, no. 1 (2014): 51–63. http://dx.doi.org/10.3109/00365513.2014.965738.

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19

Irani, Yazad, Pierre Scotney, Andrew Nash, and Keryn A. Williams. "Species Cross-Reactivity of Antibodies Used to Treat Ophthalmic Conditions." Investigative Opthalmology & Visual Science 57, no. 2 (2016): 586. http://dx.doi.org/10.1167/iovs.15-18239.

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Hansen, Tine K., Carsten Bindslev-Jensen, Per Stahl Skov, and Lars K. Poulsen. "Codfish Allergy in Adults: IgE Cross-Reactivity Among Fish Species." Annals of Allergy, Asthma & Immunology 78, no. 2 (1997): 187–94. http://dx.doi.org/10.1016/s1081-1206(10)63386-8.

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21

Plunkett, Greg A., and Michelle L. Bolner. "Defining the Extent of Allergenic Cross-reactivity among Mold Species." Journal of Allergy and Clinical Immunology 139, no. 2 (2017): AB254. http://dx.doi.org/10.1016/j.jaci.2016.12.819.

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22

Palmer, Lee K., Justin T. Marsh, Mei Lu, Richard E. Goodman, Michael G. Zeece, and Philip E. Johnson. "Shellfish Tropomyosin IgE Cross‐Reactivity Differs Among Edible Insect Species." Molecular Nutrition & Food Research 64, no. 8 (2020): 1900923. http://dx.doi.org/10.1002/mnfr.201900923.

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23

Abdullah, Mai Shihah, Ghassan Hadi Kttafah, and Muhammad Haidar Nasuruddin. "ALLERGENIC POTENTIAL AND CROSS-REACTIVITY OF FUNGAL SPECIES ISOLATED FROM THE INDOOR ENVIRONMENT." Jurnal Teknologi 84, no. 3 (2022): 47–57. http://dx.doi.org/10.11113/jurnalteknologi.v84.17742.

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Indoor fungi are potential sensitizing agents. Their detection and quantiﬁcation in indoor environments are important in the diagnosis and environmental management of fungal allergies. This study aims to analyse the allergenic potential of ten fungal species and the cross-reactivity of the two most common fungi isolated from the indoor environment samples from Sultan Idris Education University buildings. Employing in vivo (skin prick test) and in vitro (immunoblotting), the major and minor allergenic proteins of ten fungi sensitized subjects were identified. Aspergillus fumigatus and Penicilli

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24

Vanroye, Fien, Dorien Van den Bossche, Isabel Brosius, Bieke Tack, Marjan Van Esbroeck, and Jan Jacobs. "COVID-19 Antibody Detecting Rapid Diagnostic Tests Show High Cross-Reactivity When Challenged with Pre-Pandemic Malaria, Schistosomiasis and Dengue Samples." Diagnostics 11, no. 7 (2021): 1163. http://dx.doi.org/10.3390/diagnostics11071163.

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COVID-19 Antibody Detecting Rapid Diagnostic Tests (COVID-19 Ab RDTs) are the preferred tool for SARS-CoV-2 seroprevalence studies, particularly in low- and middle-income countries. The present study challenged COVID-19 Ab RDTs with pre-pandemic samples of patients exposed to tropical pathogens. A retrospective study was performed on archived serum (n = 94) and EDTA whole blood (n = 126) samples obtained during 2010–2018 from 196 travelers with malaria (n = 170), schistosomiasis (n = 25) and dengue (n = 25). COVID-19 Ab RDTs were selected based on regulatory approval status, independent evalua

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25

Smith, Roger, Joyce C. Kapatsa, Sidney J. Sherwood, Thomas A. Ficht, Joe W. Templeton, and L. Garry Adams. "Differential reactivity of bovine lymphocytes to species of Brucella." American Journal of Veterinary Research 51, no. 4 (1990): 518–23. http://dx.doi.org/10.2460/ajvr.1990.51.04.518.

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SUMMARY The reactivity of bovine lymphocytes to 4 species of Brucella was tested in thymidine-uptake assays, using long-term cultured lymphocytes and freshly obtained blood mononuclear cells. Lymphocytes were taken from cows that had been challenge exposed with a virulent strain of B abortus at midgestation. The cows were classified retrospectively as being naturally resistant or susceptible to brucellosis. Lymphocytes taken from these cows had 3 patterns of reactivity with species of Brucella: pattern 1 was defined by reactivity with 4 species (B abortus, B canis, B suis, and B melitensis); p

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26

Ledsgaard, Line, Timothy Jenkins, Kristian Davidsen, et al. "Antibody Cross-Reactivity in Antivenom Research." Toxins 10, no. 10 (2018): 393. http://dx.doi.org/10.3390/toxins10100393.

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Antivenom cross-reactivity has been investigated for decades to determine which antivenoms can be used to treat snakebite envenomings from different snake species. Traditionally, the methods used for analyzing cross-reactivity have been immunodiffusion, immunoblotting, enzyme-linked immunosorbent assay (ELISA), enzymatic assays, and in vivo neutralization studies. In recent years, new methods for determination of cross-reactivity have emerged, including surface plasmon resonance, antivenomics, and high-density peptide microarray technology. Antivenomics involves a top-down assessment of the to

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27

Dimitrov, Ivan, and Mariana Atanasova. "AllerScreener – A Server for Allergenicity and Cross-Reactivity Prediction." Cybernetics and Information Technologies 20, no. 6 (2020): 175–84. http://dx.doi.org/10.2478/cait-2020-0071.

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Abstract Allergenicity of proteins is a subtle property encoded in their structures. The prediction of allergenicity of novel proteins saves time and resources for subsequent experimental work. In the host antigen-presenting cells, the allergens are processed as antigens by the means of Human Leukocyte Antigens (HLA) class II proteins. Sometimes, people allergic to a given protein show allergic reaction to a different protein, even when the two proteins have different routes of exposure. This phenomenon is termed cross-reactivity. Here, we describe a server for allergenicity and cross-reactivi

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28

GONDIM, LUÍS F. P., JOSÉ R. MINEO, and GEREON SCHARES. "Importance of serological cross-reactivity amongToxoplasma gondii, Hammondiaspp.,Neosporaspp.,Sarcocystisspp. andBesnoitia besnoiti." Parasitology 144, no. 7 (2017): 851–68. http://dx.doi.org/10.1017/s0031182017000063.

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SUMMARYToxoplasma gondii, Neosporaspp.,Sarcocystisspp.,Hammondiaspp. andBesnoitia besnoitiare genetically related cyst-forming coccidia. Serology is frequently used for the identification ofT. gondii, Neosporaspp. andB. besnoiti-exposed individuals. Serologic cross-reactions occur in different tests among animals infected withT. gondiiandH. hammondi,as well as among animals infected byT. gondiiandN. caninum. Infections caused byN. caninumandN. hughesiare almost indistinguishable by serology.Neospora caninum, B. besnoitiandSarcocystisspp. infections in cattle show some degree of serologic cross

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29

Watts, M., N. W. Pankhurst, A. Pryce, and B. Sun. "Vitellogenin isolation, purification and antigenic cross-reactivity in three teleost species." Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 134, no. 3 (2003): 467–76. http://dx.doi.org/10.1016/s1096-4959(02)00288-9.

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30

Farady, Christopher J., Benjamin D. Sellers, Matthew P. Jacobson, and Charles S. Craik. "Improving the species cross-reactivity of an antibody using computational design." Bioorganic & Medicinal Chemistry Letters 19, no. 14 (2009): 3744–47. http://dx.doi.org/10.1016/j.bmcl.2009.05.005.

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31

Tanaka, Gabriela D., Osvaldo Augusto Sant'Anna, José Roberto Marcelino, Ana Cristina Lustoza da Luz, Marisa Maria Teixeira da Rocha, and Denise V. Tambourgi. "Micrurus snake species: Venom immunogenicity, antiserum cross-reactivity and neutralization potential." Toxicon 117 (July 2016): 59–68. http://dx.doi.org/10.1016/j.toxicon.2016.03.020.

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MIJAV, H., M. BURTON, and N. YOUNG. "168 Cross-reactivity of extracts of cladosporium species and alternaria alternata." Journal of Allergy and Clinical Immunology 87, no. 1 (1991): 180. http://dx.doi.org/10.1016/0091-6749(91)91451-x.

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FAIRLIE-CLARKE, KAREN J., CHRISTINA HANSEN, JUDITH E. ALLEN, and ANDREA L. GRAHAM. "Increased exposure to Plasmodium chabaudi antigens sustains cross-reactivity and avidity of antibodies binding Nippostrongylus brasiliensis: dissecting cross-phylum cross-reactivity in a rodent model." Parasitology 142, no. 14 (2015): 1703–14. http://dx.doi.org/10.1017/s0031182015001390.

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SUMMARYMounting an antibody response capable of discriminating amongst and appropriately targeting different parasites is crucial in host defence. However, cross-reactive antibodies that recognize (bind to) multiple parasite species are well documented. We aimed to determine if a higher inoculating dose of one species, and thus exposure to larger amounts of antigen over a longer period of time, would fine-tune responses to that species and reduce cross-reactivity. Using the Plasmodium chabaudi chabaudi (Pcc)–Nippostrongylus brasiliensis (Nb) co-infection model in BALB/c mice, in which we previ

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34

Canettieri, Antonio Carlos Victor, Fujiko Yamasiro Kretchetoff, Cristiane Yumi Koga-Ito, Daniella Moreira, Fabio José Condino Fujarra, and Carmelinda Schmidt Unterkircher. "Production of monoclonal antibodies against Streptococcus mutans antigens." Brazilian Oral Research 20, no. 4 (2006): 297–302. http://dx.doi.org/10.1590/s1806-83242006000400003.

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Several studies have been conducted in the last decades aiming to obtain an anti-caries vaccine, however some studies have demonstrated cross reactivity between Streptococcus mutans surface antigens and the human cardiac tissue. In this work, the reactivity of five anti-Streptococcus mutans monoclonal antibodies (MoAb) (24A, 56G, C8, E8 and F6) was tested against oral streptococci, cardiac antigens and skeletal and cardiac myosins, aiming to evaluate the specificity of these MoAb. The hybrid producers of immunoglobulins of the IgG2b class were cloned by limit dilution and expanded in vivo. MoA

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Grifoni, Alba, Hannah Voic, John Sidney, et al. "Crosseactivity of flaviviruses specific CD8+T cell responses across different viral species." Journal of Immunology 202, no. 1_Supplement (2019): 76.12. http://dx.doi.org/10.4049/jimmunol.202.supp.76.12.

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Abstract Several flaviviruses, including Dengue Virus (DENV), Zika Virus (ZIKV), Japanese Encephalitis Virus (JEV), West Nile Virus (WNV), and Yellow Fever Virus (YFV), share significant sequence homology and often circulate in the same geographical regions. Significant levels of cross-reactivity could in turn result in pre-existing T cell immunity modulating T cell responses to subsequent flavivirus infections or vaccination. Whether and to what extent cross-reactivity at the level of CD8 responses is detected is currently unclear. Thus we designed pools of epitopes and predicted HLA binding

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36

Huang, Zhidao, Michelle E. Akana, Kyana M. Sanders, and Daniel J. Weix. "A decarbonylative approach to alkylnickel intermediates and C(sp ³ )-C(sp ³ ) bond formation." Science 385, no. 6715 (2024): 1331–37. http://dx.doi.org/10.1126/science.abi4860.

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The myriad nickel-catalyzed cross-coupling reactions rely on the formation of an organonickel intermediate, but limitations in forming monoalkylnickel species have limited options for C(sp 3 ) cross-coupling. The formation of monoalkylnickel(II) species from abundant carboxylic acid esters would be valuable, but carboxylic acid derivatives are primarily decarboxylated to form alkyl radicals that lack the correct reactivity. In this work, we disclose a facile oxidative addition and decarbonylation sequence that forms monoalkylnickel(II) intermediates through a nonradical process. The key ligand

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37

Nollens, Hendrik H., Carolina Ruiz, Michael T. Walsh, et al. "Cross-Reactivity between Immunoglobulin G Antibodies of Whales and Dolphins Correlates with Evolutionary Distance." Clinical and Vaccine Immunology 15, no. 10 (2008): 1547–54. http://dx.doi.org/10.1128/cvi.00219-08.

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ABSTRACT Growing morphological and molecular evidence indicates that the porpoises, dolphins, and whales evolved within the even-toed ungulates, formerly known as Artiodactyla. These animals are now grouped in the Cetartiodactyla. We evaluated the antigenic similarity of the immunoglobulin G (IgG) molecules of 15 cetacean species and the domestic cow. The similarity was scored using three distinct antibodies raised against bottlenose dolphin (Tursiops truncatus) IgG in a Western blot, an indirect enzyme-linked immunosorbent assay (ELISA), and a competitive ELISA format. A score was generated f

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Afong, Michael, Kimberley A. Olynyk, Hasmukh V. Patel, John Arnold, Shuen-Kuei Liao, and Karl B. Freeman. "Immunological studies of the uncoupling protein of brown adipose tissue." Canadian Journal of Biochemistry and Cell Biology 63, no. 2 (1985): 96–101. http://dx.doi.org/10.1139/o85-014.

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The immunological relationship of the uncoupling protein from brown adipose tissue of several mammalian species was examined by using a rabbit antibody preparation against the rat protein. Complete cross-reactivity of the antibody to the protein from hamster, mouse, and rat was found, whereas the protein from rabbit cross-reacted only 25%. Cross-reactivity was also found with the human uncoupling protein, although the human protein was found to be about 1 kdalton smaller than the rat protein. No protein of the size of the uncoupling protein was detected in several tumor cell lines examined.

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Yamada, Yohko, Koji Okamoto, and Ikuo Takeuchi. "Comparison of spore proteins among species of the cellular slime moulds Dictyostelium and Polysphondylium as examined by immunological cross-reactivity." Canadian Journal of Microbiology 34, no. 7 (1988): 891–96. http://dx.doi.org/10.1139/m88-154.

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Spore proteins of six cellular slime mould species, Dictyostelium discoideum, D. mucoroides, D. purpureum, D. lacteum, Polysphondylium violaceum, and P. pallidum were studied. The spore proteins were cross-reacted with four different polyclonal antibodies produced against D. mucoroides spores and D. discoideum major spore coat proteins SP96, SP70, and SP60 by SDS polyacrylamide gel electrophoresis and immunoblotting. The spore proteins of D. discoideum and D. mucoroides showed the strongest cross-reactivity with all the antisera and also produced many common protein bands, thus reflecting thei

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Fleischauer, Valerie E., Salvador B. Muñoz III, Peter G. N. Neate, William W. Brennessel, and Michael L. Neidig. "NHC and nucleophile chelation effects on reactive iron(ii) species in alkyl–alkyl cross-coupling." Chemical Science 9, no. 7 (2018): 1878–91. http://dx.doi.org/10.1039/c7sc04750a.

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41

Borel, Nicole, Nicola Casson, José M. Entenza, Carmen Kaiser, Andreas Pospischil, and Gilbert Greub. "Tissue microarray and immunohistochemistry as tools for evaluation of antibodies against Chlamydia-like bacteria." Journal of Medical Microbiology 58, no. 7 (2009): 863–66. http://dx.doi.org/10.1099/jmm.0.009159-0.

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Tissue microarray technology was used to establish immunohistochemistry protocols and to determine the specificity of new antisera against various Chlamydia-like bacteria for future use on formalin-fixed and paraffin-embedded tissues. The antisera exhibited strong reactivity against autologous antigen and closely related heterologous antigen, but no cross-reactivity with distantly related species.

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42

Abeck, D., A. P. Johnson, and D. Taylor-Robinson. "Antigenic analysis ofHaemophilus ducreyiby Western blotting." Epidemiology and Infection 101, no. 1 (1988): 151–57. http://dx.doi.org/10.1017/s0950268800029319.

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SUMMARYTwenty-one strains ofHaemophilus ducreyiwere analysed by Western blotting using two antisera produced in mice. Common antigens of molecular weights 58, 46, 41, 28, 22 and 16 kDa were detected in all the strains. The antigens were protein in nature, since they could not be detected in whole-cell lysates which had been treated with proteinase K. TheH. ducreyistrains showed antigenic cross-reactivity with strains ofH. influenzaeandH. parainfluenzae, but showed minimal or no cross-reactivity with seven other species of bacteria.

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Ochiai, Yoshihiro, Teruki Kobayashi, Akihiro Handa, Shugo Watabe, and Kanehisa Hashimoto. "Immunological cross-reactivity of myosin light chains from various species of fish." NIPPON SUISAN GAKKAISHI 55, no. 12 (1989): 2151–56. http://dx.doi.org/10.2331/suisan.55.2151.

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44

Bonura, Angela, Anna Artale, Mauro Marino, et al. "Cross-reactivity between Parietaria species using the major rParj1 and rParj2 allergens." Allergy and Asthma Proceedings 27, no. 5 (2006): 378–82. http://dx.doi.org/10.2500/aap.2006.27.2927.

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Restani, P., A. Fiocchi, B. Beretta, T. Velonà, M. Giovannini, and C. L. Galli. "Meat allergy: III—Proteins involved and cross-reactivity between different animal species." Journal of the American College of Nutrition 16, no. 4 (1997): 383–89. http://dx.doi.org/10.1080/07315724.1997.10718701.

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Haider, Kh Husnain, and W. H. Stimson. "Bovine cardiac troponin-I specific monoclonal antibodies which show species cross reactivity." Experimental & Molecular Medicine 28, no. 2 (1996): 71–76. http://dx.doi.org/10.1038/emm.1996.11.

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Fichorova, R. N., L. S. Nakov, and S. D. Kyurkchiev. "Inter-species cross-reactivity of human sperm antibodies demonstrated by immunoenzyme method." Journal of Reproductive Immunology 15 (July 1989): 55. http://dx.doi.org/10.1016/0165-0378(89)90129-0.

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Zhao, Xin, Thiago Luiz Alves e. Silva, Laura Cronin, et al. "Immunogenicity and Serological Cross-Reactivity of Saliva Proteins among Different Tsetse Species." PLOS Neglected Tropical Diseases 9, no. 8 (2015): e0004038. http://dx.doi.org/10.1371/journal.pntd.0004038.

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UCHIDA, Tatsuya, HASBULLAH, Takashi NAKAMURA, Yutaka NAKAI, and Keiji OGIMOTO. "Cross Reactivity of Serum Antibodies from Chickens Immunized with Three Eimerian Species." Journal of Veterinary Medical Science 56, no. 5 (1994): 1021–23. http://dx.doi.org/10.1292/jvms.56.1021.

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Nishikawa, A. K., C. P. Caricati, M. L. S. R. Lima, et al. "Antigenic cross-reactivity among the venoms from several species of Brazilian scorpions." Toxicon 32, no. 8 (1994): 989–98. http://dx.doi.org/10.1016/0041-0101(94)90377-8.

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