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Journal articles on the topic 'Neisserial heparin binding antigen'

Author: Grafiati

Published: 14 March 2023

Last updated: 31 July 2025

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1

Savitskaya, Viktoriia Yu, Nina G. Dolinnaya, Vadim V. Strekalovskikh, et al. "Bioinformatics Analysis of Global Diversity in Meningococcal Vaccine Antigens over the Past 10 Years: Vaccine Efficacy Prognosis." Medical Sciences 11, no. 4 (2023): 76. http://dx.doi.org/10.3390/medsci11040076.

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Neisseria meningitidis (N. meningitidis) serogroup B (MenB) is the leading cause of invasive meningococcal disease worldwide. The pathogen has a wide range of virulence factors, which are potential vaccine components. Studying the genetic variability of antigens within a population, especially their long-term persistence, is necessary to develop new vaccines and predict the effectiveness of existing ones. The multicomponent 4CMenB vaccine (Bexsero), used since 2014, contains three major genome-derived recombinant proteins: factor H-binding protein (fHbp), Neisserial Heparin-Binding Antigen (NH

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Lucidarme, Jay, Stefanie Gilchrist, Lynne S. Newbold, et al. "Genetic Distribution of Noncapsular Meningococcal Group B Vaccine Antigens in Neisseria lactamica." Clinical and Vaccine Immunology 20, no. 9 (2013): 1360–69. http://dx.doi.org/10.1128/cvi.00090-13.

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ABSTRACTThe poor immunogenicity of the meningococcal serogroup B (MenB) capsule has led to the development of vaccines targeting subcapsular antigens, in particular the immunodominant and diverse outer membrane porin, PorA. These vaccines are largely strain specific; however, they offer limited protection against the diverse MenB-associated diseases observed in many industrialized nations. To broaden the scope of its protection, the multicomponent vaccine (4CMenB) incorporates a PorA-containing outer membrane vesicle (OMV) alongside relatively conserved recombinant protein components, includin

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Semchenko, Evgeny A., Tsitsi D. Mubaiwa, Christopher J. Day, and Kate L. Seib. "Role of the Gonococcal Neisserial Heparin Binding Antigen in Microcolony Formation, and Serum Resistance and Adherence to Epithelial Cells." Journal of Infectious Diseases 221, no. 10 (2019): 1612–22. http://dx.doi.org/10.1093/infdis/jiz628.

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Abstract The sexually transmitted infection gonorrhoea is on the rise worldwide and an increased understanding of the mechanisms of colonization and pathogenesis of Neisseria gonorrhoeae is required to aid development of new treatment and prevention strategies. In the current study, we investigate the neisserial heparin-binding antigen (NHBA) of N. gonorrhoeae and confirm its role in binding to several glycans, including heparin, and identify interactions of NHBA with both gonococcal and host cells. Furthermore, we report that a gonococcal nhba mutant displays decreased cell aggregation and mi

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Vacca, Irene, Elena Del Tordello, Gianmarco Gasperini, et al. "Neisserial Heparin Binding Antigen (NHBA) Contributes to the Adhesion of Neisseria meningitidis to Human Epithelial Cells." PLOS ONE 11, no. 10 (2016): e0162878. http://dx.doi.org/10.1371/journal.pone.0162878.

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Semchenko, Evgeny A., Aimee Tan, Ray Borrow, and Kate L. Seib. "The Serogroup B Meningococcal Vaccine Bexsero Elicits Antibodies to Neisseria gonorrhoeae." Clinical Infectious Diseases 69, no. 7 (2018): 1101–11. http://dx.doi.org/10.1093/cid/ciy1061.

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Abstract Background Neisseria gonorrhoeae and Neisseria meningitidis are closely-related bacteria that cause a significant global burden of disease. Control of gonorrhoea is becoming increasingly difficult, due to widespread antibiotic resistance. While vaccines are routinely used for N. meningitidis, no vaccine is available for N. gonorrhoeae. Recently, the outer membrane vesicle (OMV) meningococcal B vaccine, MeNZB, was reported to be associated with reduced rates of gonorrhoea following a mass vaccination campaign in New Zealand. To probe the basis for this protection, we assessed the cross

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Soler-Garcia, Aleix, Mariona Fernández de Sevilla, Raquel Abad, et al. "Meningococcal Serogroup B Disease in Vaccinated Children." Journal of the Pediatric Infectious Diseases Society 9, no. 4 (2019): 454–59. http://dx.doi.org/10.1093/jpids/piz071.

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Abstract Background Neisseria meningitidis serogroup B (MenB) is the most frequent cause of invasive meningococcal disease (IMD) in Spain. The multicomponent vaccine against MenB (4CMenB) was approved in Spain in January 2014. Methods We present 4 cases of children who developed MenB-associated IMD despite previous vaccination with 4CMenB. Extensive immunologic diagnostic work-up was performed in order to rule out any immunodeficiency. Also, molecular characterization of the MenB strain was conducted to determine whether bacterial antigens matched vaccine antigens. Results Among the 4 patients

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Corrado, Alessio, Mila Toppazzini, Alessandro Vadi, et al. "Analytical Insights into Protein–Alum Interactions and Their Impact on Conformational Epitope." Pharmaceutics 16, no. 3 (2024): 420. http://dx.doi.org/10.3390/pharmaceutics16030420.

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Several alum-adjuvanted vaccines have been licensed in the past 40 years. Despite its extensive and continuous use, the immune mechanism of action of alum adjuvants is not yet completely understood. Many different variables during the formulation process have been assessed as critical for alum-adjuvanted vaccines, although most of them are still not yet fully understood. The absence of a clear understanding of all the possible variables regulating the mechanism of action and the behavior that alum adjuvant imposes on the protein antigen may also be related to analytical challenges. For this re

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Ispasanie, Emma, Gerd Pluschke, Abraham Hodgson, Ali Sie, Calman MacLennan, and Oliver Koeberling. "Characterization of vaccine antigens of meningococcal serogroup W isolates from Ghana and Burkina Faso from 2003 to 2009." F1000Research 3 (November 3, 2014): 264. http://dx.doi.org/10.12688/f1000research.3881.1.

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Neisseria meningitidis is a major cause of bacterial meningitis and a considerable health problem in the 25 countries of the ‘African Meningitis Belt’ that extends from Senegal in West Africa to Ethiopia in the East. Approximately 80% of cases of meningococcal meningitis in Africa have been caused by strains belonging to capsular serogroup A. After the introduction of a serogroup A conjugate polysaccharide vaccine, MenAfriVac™, that began in December 2010, the incidence of meningitis due to serogroup A has markedly declined in this region. Currently, serogroup W of N. meningitidis accounts for

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Plikaytis, Brian D., Maria Stella, Giuseppe Boccadifuoco, et al. "Interlaboratory Standardization of the Sandwich Enzyme-Linked Immunosorbent Assay Designed for MATS, a Rapid, Reproducible Method for Estimating the Strain Coverage of Investigational Vaccines." Clinical and Vaccine Immunology 19, no. 10 (2012): 1609–17. http://dx.doi.org/10.1128/cvi.00202-12.

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ABSTRACTThe meningococcal antigen typing system (MATS) sandwich enzyme-linked immunosorbent assay (ELISA) was designed to measure the immunologic cross-reactivity and quantity of antigens in target strains of a pathogen. It was first used to measure the factor H-binding protein (fHbp), neisserial adhesin A (NadA), and neisserial heparin-binding antigen (NHBA) content of serogroup B meningococcal (MenB) isolates relative to a reference strain, or “relative potency” (RP). With the PorA genotype, the RPs were then used to assess strain coverage by 4CMenB, a multicomponent MenB vaccine. In prelimi

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Maritan, Martina, Roberta Cozzi, Paola Lo Surdo, Daniele Veggi, Matthew James Bottomley, and Enrico Malito. "Crystal structures of human Fabs targeting the Bexsero meningococcal vaccine antigen NHBA." Acta Crystallographica Section F Structural Biology Communications 73, no. 6 (2017): 305–14. http://dx.doi.org/10.1107/s2053230x17006021.

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Neisserial heparin-binding antigen (NHBA) is a surface-exposed lipoprotein fromNeisseria meningitidisand is a component of the meningococcus B vaccine Bexsero. As part of a study to characterize the three-dimensional structure of NHBA and the molecular basis of the human immune response to Bexsero, the crystal structures of two fragment antigen-binding domains (Fabs) isolated from human monoclonal antibodies targeting NHBA were determined. Through a high-resolution analysis of the organization and the amino-acid composition of the CDRs, these structures provide broad insights into the NHBA epi

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Vu, David M., Tracy T. Wong, and Dan M. Granoff. "Cooperative serum bactericidal activity between human antibodies to meningococcal factor H binding protein and Neisserial heparin binding antigen." Vaccine 29, no. 10 (2011): 1968–73. http://dx.doi.org/10.1016/j.vaccine.2010.12.075.

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Newcombe, Jane, Tom A. Mendum, Chuan-peng Ren, and Johnjoe McFadden. "Identification of the immunoproteome of the meningococcus by cell surface immunoprecipitation and MS." Microbiology 160, no. 2 (2014): 429–38. http://dx.doi.org/10.1099/mic.0.071829-0.

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Most healthy adults are protected from meningococcal disease by the presence of naturally acquired anti-meningococcal antibodies; however, the identity of the target antigens of this protective immunity remains unclear, particularly for protection against serogroup B disease. To identify the protein targets of natural protective immunity we developed an immunoprecipitation and proteomics approach to define the immunoproteome of the meningococcus. Sera from 10 healthy individuals showing serum bactericidal activity against both a meningococcal C strain (L91543) and the B strain MC58, together w

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Domina, Maria, Veronica Lanza Cariccio, Salvatore Benfatto, et al. "Epitope Mapping of a Monoclonal Antibody Directed against Neisserial Heparin Binding Antigen Using Next Generation Sequencing of Antigen-Specific Libraries." PLOS ONE 11, no. 8 (2016): e0160702. http://dx.doi.org/10.1371/journal.pone.0160702.

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Semchenko, Evgeny A., Christopher J. Day, and Kate L. Seib. "The Neisseria gonorrhoeae Vaccine Candidate NHBA Elicits Antibodies That Are Bactericidal, Opsonophagocytic and That Reduce Gonococcal Adherence to Epithelial Cells." Vaccines 8, no. 2 (2020): 219. http://dx.doi.org/10.3390/vaccines8020219.

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Due to the continuing emergence of multidrug resistant strains of Neisseria gonorrhoeae there is an urgent need for the development of a gonococcal vaccine. We evaluated the gonococcal Neisseria heparin binding antigen (NHBA) as a potential vaccine candidate, in terms of its sequence conservation and expression in a range of N. gonorrhoeae strains, as well as its immunogenicity and the functional activity of antibodies raised to either the full length NHBA or a C-terminal fragment of NHBA (NHBA-c). The gene encoding NHBA is highly conserved and expressed in all N. gonorrhoeae strains investiga

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15

Abad, R., A. Biolchi, M. Moschioni, M. M. Giuliani, M. Pizza, and J. A. Vázquez. "A Large Portion of Meningococcal Antigen Typing System-Negative Meningococcal Strains from Spain Is Killed by Sera from Adolescents and Infants Immunized with 4CMenB." Clinical and Vaccine Immunology 22, no. 4 (2015): 357–60. http://dx.doi.org/10.1128/cvi.00669-14.

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ABSTRACTA new vaccine (the 4CMenB 4-component protein vaccine [Bexsero], which includes PorA, factor H-binding protein [fHbp], neisserial heparin-binding antigen [NHBA], andNeisseriaadhesin A [NadA]) against serogroup B meningococci has recently been approved for use in people older than age 2 months in Europe, Australia, and Canada. Preapproval clinical efficacy studies are not feasible for invasive meningococcal disease because its incidence is low/very low, and the serum bactericidal antibody (SBA) titer (or the human SBA [hSBA] titer when human complement is used in the assay) has been use

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Rossi, Raffaella, Peter T. Beernink, Serena Giuntini, and Dan M. Granoff. "Susceptibility of Meningococcal Strains Responsible for Two Serogroup B Outbreaks on U.S. University Campuses to Serum Bactericidal Activity Elicited by the MenB-4C Vaccine." Clinical and Vaccine Immunology 22, no. 12 (2015): 1227–34. http://dx.doi.org/10.1128/cvi.00474-15.

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ABSTRACTIn 2013 and 2014, two U.S. universities had meningococcal serogroup B outbreaks (a total of 14 cases) caused by strains from two different clonal complexes. To control the outbreaks, students were immunized with a serogroup B meningococcal vaccine (Novartis) that was not yet licensed in the United States. The vaccine (referred to as MenB-4C) contains four components capable of eliciting bactericidal activity. Both outbreak strains had high expression levels of two of the vaccine antigens (subfamily B factor H binding protein [FHbp] and neisserial heparin binding antigen [NHba]); the un

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Garcia, Yara Ruiz, Woo-Yun Sohn, Mariagrazia Pizza, and Rafik Bekkat-Berkani. "02. Beyond B Antigen Coverage: The Potential of the 4CMenB Vaccine for Cross-protection Against Pathogenic Neisseria Infections." Open Forum Infectious Diseases 8, Supplement_1 (2021): S125. http://dx.doi.org/10.1093/ofid/ofab466.205.

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Abstract Background Two human pathogenic Neisseria species exist: N. meningitidis (Nm) and N. gonorrhoeae (Ng). Although causing disparate clinical syndromes, invasive meningococcal disease (IMD) and gonorrhea, they are genetically similar and share key protein antigens. The 4CMenB vaccine, licensed against meningococcal B disease, comprises 4 antigenic components (factor H binding protein (fHbp), variant 1.1, subfamily B; Neisseria heparin binding antigen (NHBA) peptide 2; Neisserial adhesin A (NadA) variant 3; and Porin A (PorA) P1.4), and potentially protects against non-B invasive meningoc

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Bos, Martine P., David Kao, Daniel M. Hogan, Christopher C. R. Grant, and Robert J. Belland. "Carcinoembryonic Antigen Family Receptor Recognition by Gonococcal Opa Proteins Requires Distinct Combinations of Hypervariable Opa Protein Domains." Infection and Immunity 70, no. 4 (2002): 1715–23. http://dx.doi.org/10.1128/iai.70.4.1715-1723.2002.

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ABSTRACT Neisserial Opa proteins function as a family of adhesins that bind heparan sulfate proteoglycan (HSPG) or carcinoembryonic antigen family (CEACAM) receptors on human host cells. In order to define the CEACAM binding domain on Opa proteins, we tested the binding properties of a series of gonococcal (strain MS11) recombinants producing mutant and chimeric Opa proteins with alterations in one or more of the four surface-exposed loops. Mutagenesis demonstrated that the semivariable domain, present in the first loop, was completely dispensable for CEACAM binding. In contrast, the two hyper

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Di Fede, Martina, Massimiliano Biagini, Elena Cartocci, et al. "Neisseria Heparin Binding Antigen is targeted by the human alternative pathway C3-convertase." PLOS ONE 13, no. 3 (2018): e0194662. http://dx.doi.org/10.1371/journal.pone.0194662.

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Chen, Tie, Fritz Grunert, Andrew Medina-Marino, and Emil C. Gotschlich. "Several Carcinoembryonic Antigens (CD66) Serve as Receptors for Gonococcal Opacity Proteins." Journal of Experimental Medicine 185, no. 9 (1997): 1557–64. http://dx.doi.org/10.1084/jem.185.9.1557.

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Neisseria gonorrhoeae (GC) is a human pathogen that adheres to and invades genital surfaces. Although pili are required for the initial adherence, the interaction of GC with epithelial cells is also promoted by a family of outer membrane proteins, the opacity (Opa) proteins such as OpaA protein from strain MS11. Studies have demonstrated that the interaction of the OpaA GC with epithelial cells involves binding to heparan sulfate attached to syndecan receptors. However, other Opa proteins interact with CEA gene family member 1 (CGM1) or biliary glycoprotein (BGP), members of the CD66 antigen f

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Sarantis, Helen, and Scott D. Gray-Owen. "Defining the Roles of Human Carcinoembryonic Antigen-Related Cellular Adhesion Molecules during Neutrophil Responses to Neisseria gonorrhoeae." Infection and Immunity 80, no. 1 (2011): 345–58. http://dx.doi.org/10.1128/iai.05702-11.

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ABSTRACTSymptomatic infection of humans withNeisseria gonorrhoeaeis characterized by a neutrophil-rich cervical or urethral exudate, suggesting that neutrophils are important both for the clearance of these bacteria and for the pathogenesis of gonorrhea.Neisseriainteracts with neutrophils through ligation of human carcinoembryonic antigen related-cellular adhesion molecules (CEACAMs) by their surface-expressed Opa proteins, resulting in bacterial binding, engulfment, and neutrophil activation. Multiple CEACAMs are expressed by human neutrophils, and yet their coexpression has precluded underst

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NAITO, Mariko, Tomohiko FUKUDA, Kiyotoshi SEKIGUCHI та Takeshi YAMADA. "The domains of human fibronectin mediating the binding of α antigen, the most immunopotent antigen of mycobacteria that induces protective immunity against mycobacterial infection". Biochemical Journal 347, № 3 (2000): 725–31. http://dx.doi.org/10.1042/bj3470725.

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We have recently shown that α antigen (α-Ag), the immunodominant antigen of mycobacteria, has a novel fibronectin (FN)-binding motif that is unique among mycobacteria [Naito, Ohara, Matsumoto and Yamada (1998) J. Biol. Chem. 273, 2905-2909]. In this study, we examined the domains of human FN that interacted with α-Ag. Fragments of FN generated by either proteolysis or recombinant DNA techniques were compared for their ability to bind to α-Ag. Fragments containing either the C-terminal heparin-binding domain or the central cell-binding domain consistently bound to α-Ag. The fragment of the C-te

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Sakuma, T., S. Higashiyama, S. Hosoe, S. Hayashi, and N. Taniguchi. "CD9 Antigen Interacts with Heparin-Binding EGF-Like Growth Factor through Its Heparin-Binding Domain." Journal of Biochemistry 122, no. 2 (1997): 474–80. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a021776.

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Sekiguchi, Asuka, Miwako Narita, Toshio Yano, et al. "Enhancing Effects of Heparin/Low Molecular Weight Heparin/Heparan Sulfate on Antigen Presentation and Antigen-Specific Cytotoxic T Lymphocyte (CTL) Induction by Monocyte-Derived Dendritic Cells." Blood 104, no. 11 (2004): 3816. http://dx.doi.org/10.1182/blood.v104.11.3816.3816.

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Abstract Heparin is bound with heparin-binding sites on certain cells, which induces proliferation and differentiation signals. In addition, heparin is bound with heparin-binding domains of various cytokines, which enhances the interaction between cytokines and target cells. Monocytes have been demonstrated to posses heparin-binding sites on cell surfaces. In the present study, we investigated the effects of heparin (including low molecular weight heparin) and heparan sulfate on antigen presentation and antigen-specific CTL induction of monocyte-derived DCs. Peripheral blood CD14+ cells were c

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Lujan, Eduardo, Rolando Pajon, and Dan M. Granoff. "Impaired Immunogenicity of Meningococcal Neisserial Surface Protein A in Human Complement Factor H Transgenic Mice." Infection and Immunity 84, no. 2 (2015): 452–58. http://dx.doi.org/10.1128/iai.01267-15.

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Neisserial surface protein A (NspA) is a highly conserved outer membrane protein previously investigated as a meningococcal vaccine candidate. Despite eliciting serum bactericidal activity in mice, a recombinant NspA vaccine failed to elicit serum bactericidal antibodies in a phase 1 clinical trial in humans. The discordant results may be explained by the recent discovery that NspA is a human-specific ligand of the complement inhibitor factor H (FH). Therefore, in humans but not mice, NspA would be expected to form a complex with FH, which could impair human anti-NspA protective antibody respo

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Khandelwal, Sanjay, Johnson M. Alexandra, C. Garren Hester, Michael M. Frank, and Gowthami M. Arepally. "Mechanism of Complement Activation By PF4/ Heparin Complexes." Blood 128, no. 22 (2016): 137. http://dx.doi.org/10.1182/blood.v128.22.137.137.

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Abstract The mechanisms underlying the PF4/heparin immune response are poorly understood. In recent studies, we showed that PF4/heparin complexes, but not PF4 alone or heparin alone, activate complement (C') in a heparin-dependent manner and lead to selective binding of C'-coated antigen (PF4/heparin complexes) to B cells via CD21. In additional studies, we showed that heparinized patients have circulating B cells with C'-coated PF4/heparin complexes (Khandelwal, Blood 2016). To investigate the mechanism by which PF4/heparin complexes activate complement, we performed studies in whole blood us

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Jalkanen, S., and M. Jalkanen. "Lymphocyte CD44 binds the COOH-terminal heparin-binding domain of fibronectin." Journal of Cell Biology 116, no. 3 (1992): 817–25. http://dx.doi.org/10.1083/jcb.116.3.817.

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The lymphocyte-high endothelial venule (HEV) cell interaction is an essential element of the immune system, as it controls lymphocyte recirculation between blood and lymphoid organs in the body. This interaction involves an 85-95-kD class of lymphocyte surface glycoprotein(s), CD44. A subset of lymphocyte CD44 molecules is modified by covalent linkage to chondroitin sulfate (Jalkanen, S., M. Jalkanen, R. Bargatze, M. Tammi, and E. C. Butcher. 1988. J. Immunol. 141:1615-1623). In this work, we show that removal of chondroitin sulfate by chondroitinase treatment of lymphocytes or incubation of H

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Muenzner, Petra, Christoph Dehio, Taku Fujiwara, Mark Achtman, Thomas F. Meyer, and Scott D. Gray-Owen. "Carcinoembryonic Antigen Family Receptor Specificity of Neisseria meningitidis Opa Variants Influences Adherence to and Invasion of Proinflammatory Cytokine-Activated Endothelial Cells." Infection and Immunity 68, no. 6 (2000): 3601–7. http://dx.doi.org/10.1128/iai.68.6.3601-3607.2000.

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ABSTRACT The carcinoembryonic antigen (CEA) family member CEACAM1 (previously called biliary glycoprotein or CD66a) was previously shown to function as a receptor that can mediate the binding of Opa protein-expressing Neisseria meningitidis to both neutrophils and epithelial cells. Since neutrophils and polarized epithelia have both been shown to coexpress multiple CEACAM receptors, we have now extended this work to characterize the binding specificity of meningococcal Opa proteins with other CEA family members. To do so, we used recombinant Escherichia coli expressing nine different Opa varia

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Bos, Martine P., Motomu Kuroki, Anna Krop-Watorek, Daniel Hogan, and Robert J. Belland. "CD66 receptor specificity exhibited by neisserial Opa variants is controlled by protein determinants in CD66 N-domains." Proceedings of the National Academy of Sciences 95, no. 16 (1998): 9584–89. http://dx.doi.org/10.1073/pnas.95.16.9584.

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Neisseria gonorrhoeaestrain MS11 is able to express 11 different opacity (Opa) proteins on its outer surface. A number of these Opa proteins have been shown to function as adhesins through binding of CD66 receptors present on human cells. CD66 antigens, or carcinoembryonic antigen family members, constitute a family of glycoproteins belonging to the immunoglobulin superfamily. Opa variants recognize this class of receptors in a differential manner such that certain Opa variants recognize up to four different CD66 receptors (CD66a, -c, -d, and -e), whereas others recognize only two (CD66a and -

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Holen, Halvor L., Lillian Zernichow, Kristine E. Fjelland, et al. "Ephrin-B3 binds to a sulfated cell-surface receptor." Biochemical Journal 433, no. 1 (2010): 215–23. http://dx.doi.org/10.1042/bj20100865.

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The ephrins are a family of proteins known to bind the Eph (erythropoietin-producing hepatocellular) receptor tyrosine kinase family. In the present paper, we provide data showing that ephrin-B3 binds a sulfated cell-surface protein on HEK-293T (human embryonic kidney-293 cells expressing the large T-antigen of simian virus 40) and HeLa cells, a binding that is nearly completely blocked by treatment of these cell lines with chlorate or heparinase, or by addition of the heavily sulfated glycosaminoglycan heparin. This indicates that heparan sulfate on these cells is essential for cell-surface b

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Almus, FE, LV Rao, UR Pendurthi, L. Quattrochi, and SI Rapaport. "Mechanism for diminished tissue factor expression by endothelial cells cultured with heparin binding growth factor-1 and heparin." Blood 77, no. 6 (1991): 1256–62. http://dx.doi.org/10.1182/blood.v77.6.1256.1256.

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Abstract We have extended our earlier observation that growing primary cultures of human umbilical vein endothelial cells (HUVEC) with heparin binding growth factor 1 (HBGF-1) 20 micrograms/mL and heparin 12 U/mL inhibits expression of tissue factor (TF) activity on HUVC monolayers perturbed with thrombin. TF activity was measured as the ability of monolayers or cell lysates to support FVIIa-catalyzed activation peptide release from 3H-FX. TF antigen in HUVEC extracts was measured in an enzyme-linked immunosorbent assay (ELISA) that uses a double-antibody sandwich technique with rabbit and goa

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Almus, FE, LV Rao, UR Pendurthi, L. Quattrochi, and SI Rapaport. "Mechanism for diminished tissue factor expression by endothelial cells cultured with heparin binding growth factor-1 and heparin." Blood 77, no. 6 (1991): 1256–62. http://dx.doi.org/10.1182/blood.v77.6.1256.bloodjournal7761256.

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We have extended our earlier observation that growing primary cultures of human umbilical vein endothelial cells (HUVEC) with heparin binding growth factor 1 (HBGF-1) 20 micrograms/mL and heparin 12 U/mL inhibits expression of tissue factor (TF) activity on HUVC monolayers perturbed with thrombin. TF activity was measured as the ability of monolayers or cell lysates to support FVIIa-catalyzed activation peptide release from 3H-FX. TF antigen in HUVEC extracts was measured in an enzyme-linked immunosorbent assay (ELISA) that uses a double-antibody sandwich technique with rabbit and goat antibod

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Kavan, Daniel, Markéta Vančurová, Dana Ulbrichová, Ivana Hladíková, Miloslav Pospíšil, and Karel Bezouška. "Identification of Heparin-Binding Sites in the Fibronectin Type III Domains of the Leukocyte Common Antigen (CD45)." Collection of Czechoslovak Chemical Communications 69, no. 3 (2004): 645–58. http://dx.doi.org/10.1135/cccc20040645.

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Leukocyte common antigens (CD45) are large receptors that are abundantly expressed at the surface of all leukocytes. These receptors are type I membrane glycoproteins possessing two large C-terminal intracellular domains with protein tyrosine phosphatase activity. While the role of these enzyme domains in leukocyte signaling is well documented, the role of the N-terminal extracellular portion of CD45, composed of sequences formed by alternatively spliced exons, the cysteine rich domain, and three type III fibronectin repeats, remains unclear. The presence of fibronectin domains would predict t

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Krauel, Krystin, Claudia Weber, Sven Brandt, et al. "Platelet factor 4 binding to lipid A of Gram-negative bacteria exposes PF4/heparin-like epitopes." Blood 120, no. 16 (2012): 3345–52. http://dx.doi.org/10.1182/blood-2012-06-434985.

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AbstractThe positively charged chemokine platelet factor 4 (PF4) forms immunogenic complexes with heparin and other polyanions. Resulting antibodies can induce the adverse drug effect heparin-induced thrombocytopenia. PF4 also binds to bacteria, thereby exposing the same neoantigen(s) as with heparin. In this study, we identified the negatively charged lipopolysaccharide (LPS) as the PF4 binding structure on Gram-negative bacteria. We demonstrate by flow cytometry that mutant bacteria with progressively truncated LPS structures show increasingly enhanced PF4 binding activity. PF4 bound stronge

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Brissette, Catherine A., Tomasz Bykowski, Anne E. Cooley, Amy Bowman, and Brian Stevenson. "Borrelia burgdorferi RevA Antigen Binds Host Fibronectin." Infection and Immunity 77, no. 7 (2009): 2802–12. http://dx.doi.org/10.1128/iai.00227-09.

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ABSTRACT Borrelia burgdorferi, the Lyme disease-causing spirochete, can persistently infect its vertebrate hosts for years. B. burgdorferi is often found associated with host connective tissue, where it interacts with components of the extracellular matrix, including fibronectin. Some years ago, a borrelial surface protein, named BBK32, was identified as a fibronectin-binding protein. However, B. burgdorferi BBK32 mutants are still able to bind fibronectin, indicating that the spirochete possesses additional mechanisms for adherence to fibronectin. We now demonstrate that RevA, an unrelated B.

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Tripodi, A., A. Krachmalnicoff, and P. M. Mannucci. "Characterization of an Abnormal Antithrombin (Milano 2) with Defective Thrombin Binding." Thrombosis and Haemostasis 56, no. 03 (1986): 349–52. http://dx.doi.org/10.1055/s-0038-1661681.

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SummaryFour members of an Italian family (two with histories of venous thromboembolism) had a qualitative defect of antithrombin III reflected by normal antigen concentrations and halfnormal antithrombin activity with or without heparin. Anti-factor Xa activities were consistently borderline low (about 70% of normal). For the propositus’ plasma and serum the patterns of antithrombin III in crossed-immunoelectrophoresis with or without heparin were indistinguishable from those of normal plasma or serum. A normal affinity of antithrombin III for heparin was documented by heparin-sepharose chroma

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Menozzi, F. D., J. H. Rouse, M. Alavi, et al. "Identification of a heparin-binding hemagglutinin present in mycobacteria." Journal of Experimental Medicine 184, no. 3 (1996): 993–1001. http://dx.doi.org/10.1084/jem.184.3.993.

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Adherence to mammalian host tissues is an important virulence trait in microbial pathogenesis, yet little is known about the adherence mechanisms of mycobacteria. Here, we show that binding of mycobacteria to epithelial cells but not to macrophages can be specifically inhibited by sulfated carbohydrates. Using heparin-Sepharose chromatography, a 28-kD heparin-binding protein was purified from culture supernatants and cell extracts of Mycobacterium bovis and Mycobacterium tuberculosis. This protein, designated heparin-binding hemagglutinin (HBHA), promotes the agglutination of rabbit erythrocyt

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Sachais, Bruce S., Rustem I. Litvinov, Serge V. Yarovoi, et al. "Dynamic antibody-binding properties in the pathogenesis of HIT." Blood 120, no. 5 (2012): 1137–42. http://dx.doi.org/10.1182/blood-2012-01-407262.

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Abstract Rapid laboratory assessment of heparin-induced thrombocytopenia (HIT) is important for disease recognition and management. The utility of contemporary immunoassays to detect antiplatelet factor 4 (PF4)/heparin antibodies is hindered by detection of antibodies unassociated with disease. To begin to distinguish properties of pathogenic anti-PF4/heparin antibodies, we compared isotype-matched monoclonal antibodies that bind to different epitopes: KKO causes thrombocytopenia in an in vivo model of HIT, whereas RTO does not. KKO binding to PF4 and heparin is specifically inhibited by human

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Fabris, Fabrizio, Immacolata Cordiano, Federica Salvan, et al. "Heparin-Induced Thrombocytopenia: Prevalence in a Large Cohort of Patients and Confirmed Role of PF4/Heparin Complex as the Main Antigen for Antibodies." Clinical and Applied Thrombosis/Hemostasis 3, no. 3 (1997): 203–9. http://dx.doi.org/10.1177/107602969700300309.

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We performed a retrospective study on the prevalence of heparin-induced thrombocytopenia (HIT) in 233 patients receiving hog mucosa heparin therapy. Of these, 82 patients received s.c. calcium heparin, 130 patient received unfractionated (UF) i.v. heparin, and 21 patients received low molecular weight heparins (LMWH). An additional four patients, referred to our consultation and diagnosed by us as having clinically active type II HIT (HIT-II) were also studied. The mean platelet count of the 233 patients receiving heparin showed a significant decrease after 2 days of heparin treatment and a fo

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Beernink, Peter T., Arunas Leipus, and Dan M. Granoff. "Rapid Genetic Grouping of Factor H-Binding Protein (Genome-Derived Neisserial Antigen 1870), a Promising Group B Meningococcal Vaccine Candidate." Clinical and Vaccine Immunology 13, no. 7 (2006): 758–63. http://dx.doi.org/10.1128/cvi.00097-06.

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ABSTRACT The most important antigen component of a promising multicomponent group B meningococcal recombinant protein vaccine is based on genome-derived neisserial antigen 1870, which recently was renamed factor H-binding protein (FHBP) to reflect one of its critical functions as a complement regulatory protein. Neisseria meningitidis strains can be subdivided into three FHBP variant groups based on divergence of FHBP amino acid sequences. Within each variant group, amino acid sequences are >90% conserved. To develop an FHBP-based group B vaccine, it is important to know the distribution of

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Newman, Peter, Rebecca Swanson, and Beng Chong. "Heparin-induced Thrombocytopenia: IgG Binding to PF4-Heparin Complexes in the Fluid Phase and Cross-reactivity with Low Molecular Weight Heparin and Heparinoid." Thrombosis and Haemostasis 80, no. 08 (1998): 292–97. http://dx.doi.org/10.1055/s-0037-1615190.

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SummaryEarly diagnosis of heparin-induced thrombocytopenia (HIT) is essential to reduce morbidity and mortality. We report an enzyme immunoassay which detects the binding of HIT IgG to PF4-heparin in the fluid phase. Our fluid phase assay produces consistently low background and can detect low levels of anti-PF4-heparin. It is suited to testing alternative anticoagulants because, unlike in an ELISA, a clearly defined amount of antigen is available for antibody binding. We were able to detect anti-PF4-heparin IgG in 26/28 (93%) HIT patients. We investigated cross-reactivity of anti-PF4-heparin

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Radtke, Klaus-P., Judith S. Greengard, José A. Fernández, Bruno O. Villoutreix, and John H. Griffin. "A Two-Allele Polymorphism in Protein C Inhibitor with Varying Frequencies in Different Ethnic Populations." Thrombosis and Haemostasis 75, no. 01 (1996): 062–69. http://dx.doi.org/10.1055/s-0038-1650222.

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SummarycDNAs for protein C inhibitor (PCI), prepared from human liver RNA, contained two forms of PCI, designated PCI*A and PCPB 1 . While PCI*A is identical to the published PCI sequence, PCPB differs in 4 of 1221 bp and two amino acids, A36V and K86E. Frequencies for the PCI*B allele, determined from genomic DNA, differed among ethnic groups. Frequency distribution and historical migration of modem man suggest that PCI*A arose from the PCI*B allele. Antigen levels in plasma homozygous for PCI*A or PCI*B equalled that of pooled normal plasma. K86E in PCI*B causes a charge alteration in helix

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Krauel, Krystin, Christian Pötschke, Claudia Weber, et al. "Platelet factor 4 binds to bacteria, inducing antibodies cross-reacting with the major antigen in heparin-induced thrombocytopenia." Blood 117, no. 4 (2011): 1370–78. http://dx.doi.org/10.1182/blood-2010-08-301424.

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AbstractA clinically important adverse drug reaction, heparin-induced thrombocytopenia (HIT), is induced by antibodies specific for complexes of the chemokine platelet factor 4 (PF4) and the polyanion heparin. Even heparin-naive patients can generate anti-PF4/heparin IgG as early as day 4 of heparin treatment, suggesting preimmunization by antigens mimicking PF4/heparin complexes. These antibodies probably result from bacterial infections, as (1) PF4 bound charge-dependently to various bacteria, (2) human heparin-induced anti-PF4/heparin antibodies cross-reacted with PF4-coated Staphylococcus

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Li, Zhong Q., Weiyi Liu, Kwang S. Park, et al. "Defining a second epitope for heparin-induced thrombocytopenia/thrombosis antibodies using KKO, a murine HIT-like monoclonal antibody." Blood 99, no. 4 (2002): 1230–36. http://dx.doi.org/10.1182/blood.v99.4.1230.

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Heparin-induced thrombocytopenia/thrombosis (HIT/T) is a common complication of heparin therapy that is caused by antibodies to platelet factor 4 (PF4) complexed with heparin. The immune response is polyclonal and polyspecific, ie, more than one neoepitope on PF4 is recognized by HIT/T antibodies. One such epitope has been previously identified; it involves the domain between the third and fourth cysteine residues in PF4 (site 1). However, the binding sites for other HIT/T antibodies remain to be defined. To explore this issue, the binding site of KKO, an HIT/T-like murine monoclonal antibody,

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Borghi, Sara, Ana Antunes, Andreas F. Haag, et al. "Multilayer Regulation of Neisseria meningitidis NHBA at Physiologically Relevant Temperatures." Microorganisms 10, no. 4 (2022): 834. http://dx.doi.org/10.3390/microorganisms10040834.

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Neisseria meningitidis colonizes the nasopharynx of humans, and pathogenic strains can disseminate into the bloodstream, causing septicemia and meningitis. NHBA is a surface-exposed lipoprotein expressed by all N. meningitidis strains in different isoforms. Diverse roles have been reported for NHBA in heparin-mediated serum resistance, biofilm formation, and adherence to host tissues. We determined that temperature controls the expression of NHBA in all strains tested, with increased levels at 30–32 °C compared to 37 °C. Higher NHBA expression at lower temperatures was measurable both at mRNA

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Greinacher, Andreas. "Treatment of Heparin-Induced Thrombocytopenia." Thrombosis and Haemostasis 82, no. 08 (1999): 457–67. http://dx.doi.org/10.1055/s-0037-1615866.

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IntroductionUnfractionated heparin (UFH) and low molecular weight heparin (LMWH) are the most widely used anticoagulants when parenteral anticoagulation with a short half-life is required. Both can be administered subcutaneously and intravenously, and both have been shown to be effective in a variety of clinical settings.1 UFH has several limitations. One is its poor bioavailability after subcutaneous injection and the marked variability in its anticoagulant response in patients with an acute thromboembolic complication.2,3 Another major issue associated with UFH is the induction of heparin-in

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Vilstrup, Joachim, Amanda Simonsen, Thea Birkefeldt, et al. "Crystal and solution structures of fragments of the human leucocyte common antigen-related protein." Acta Crystallographica Section D Structural Biology 76, no. 5 (2020): 406–17. http://dx.doi.org/10.1107/s2059798320003885.

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Leucocyte common antigen-related protein (LAR) is a post-synaptic type I transmembrane receptor protein that is important for neuronal functionality and is genetically coupled to neuronal disorders such as attention deficit hyperactivity disorder (ADHD). To understand the molecular function of LAR, structural and biochemical studies of protein fragments derived from the ectodomain of human LAR have been performed. The crystal structure of a fragment encompassing the first four FNIII domains (LARFN1–4) showed a characteristic L shape. SAXS data suggested limited flexibility within LARFN1–4, whi

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Lee, Hannah S. W., Ian C. Boulton, Karen Reddin, et al. "Neisserial Outer Membrane Vesicles Bind the Coinhibitory Receptor Carcinoembryonic Antigen-Related Cellular Adhesion Molecule 1 and Suppress CD4+ T Lymphocyte Function." Infection and Immunity 75, no. 9 (2007): 4449–55. http://dx.doi.org/10.1128/iai.00222-07.

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ABSTRACT Pathogenic Neisseria bacteria naturally liberate outer membrane “blebs,” which are presumed to contribute to pathology, and the detergent-extracted outer membrane vesicles (OMVs) from Neisseria meningitidis are currently employed as meningococcal vaccines in humans. While the composition of these vesicles reflects the bacteria from which they are derived, the functions of many of their constituent proteins remain unexplored. The neisserial colony opacity-associated Opa proteins function as adhesins, the majority of which mediate bacterial attachment to human carcinoembryonic antigen-r

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Pu, Feifei, Jing Feng, Fei Niu, and Ping Xia. "Diagnostic value of recombinant heparin-binding hemagglutinin adhesin protein in spinal tuberculosis." Open Medicine 15, no. 1 (2020): 114–18. http://dx.doi.org/10.1515/med-2020-0017.

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AbstractBackground and aimTo explore the diagnostic value of recombinant heparin-binding hemagglutinin adhesin (HBHA) protein antigen in spinal tuberculosis.Materials and methodsForty patients with spinal tuberculosis were included in the experimental group and 40 healthy people were included in the control group. Serum IgG antibody expression level was detected with recombinant HBHA protein as the antigen, using enzyme-linked immunosorbent assay (ELISA) detection.ResultsPatients with spinal tuberculosis and healthy volunteers were included in this study. A total of 40 eligible patients with s

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Greinacher, Andreas, Susanne Alban, Veronika Dummel, Gerhard Franz, and Christian Mueller-Eckhardt. "Characterization of the Structural Requirements for a Carbohydrate Based Anticoagulant with a Reduced Risk of Inducing the Immunological Type of Heparin-associated Thrombocytopenia." Thrombosis and Haemostasis 74, no. 03 (1995): 886–92. http://dx.doi.org/10.1055/s-0038-1649842.

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SummaryHAT is the most frequent drug induced immune-thrombocytopenia. We recently identified multimolecular PF4/heparin complexes as the major antigen. In order to evaluate the structural requirements for formation of the antigenic complex, we chemically synthesized 13 glucan sulfates and used 5 heparin fractions (2.4-4.8 kD) and a synthesized pentasaccharide, representing the antithrombin III binding sequence of heparin, to further characterize the HAT antigen. In the presence of glucan sulfates and heparin, HAT antibodies caused platelet activation typically at low but not at high concentrat

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