Cross-Reactivity of Antipneumococcal Surface Protein C (PspC) Antibodies with Different Strains and Evaluation of Inhibition of Human Complement Factor H and Secretory IgA Binding via PspC

Moreno, A. T., Oliveira, M. L. S., Ho, P. L., Vadesilho, C. F. M., Palma, G. M. P., Ferreira, J. M. C., Ferreira, Daniela ORCID: https://orcid.org/0000-0002-0594-0902, Santos, S. R., Martinez, M. B. and Miyaji, E. N. (2012) 'Cross-Reactivity of Antipneumococcal Surface Protein C (PspC) Antibodies with Different Strains and Evaluation of Inhibition of Human Complement Factor H and Secretory IgA Binding via PspC'. Clinical and Vaccine Immunology, Vol 19, Issue 4, pp. 499-507.

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Abstract

Pneumococcal surface protein C (PspC) is an important candidate for a cost-effective vaccine with broad coverage against pneumococcal diseases. Previous studies have shown that Streptococcus pneumoniae is able to bind to both human factor H (FH), an inhibitor of complement alternative pathway, and human secretory IgA (sIgA) via PspC. PspC was classified into 11 groups based on variations of the gene. In this work, we used three PspC fragments from different groups (PspC3, PspC5, and PspC8) to immunize mice for the production of antibodies. Immunization with PspC3 induced antibodies that recognized the majority of the clinical isolates as analyzed by Western blotting of whole-cell extracts and flow cytometry of intact bacteria, while anti-PspC5 antibodies showed cross-reactivity with the paralogue pneumococcal surface protein A (PspA), and anti-PspC8 antibodies reacted only with the PspC8-expressing strain. Most of the isolates tested showed strong binding to FH and weaker interaction with sIgA. Preincubation with anti-PspC3 and anti-PspC5 IgG led to some inhibition of binding of FH, and preincubation with anti-PspC3 partially inhibited sIgA binding in Western blotting. The analysis of intact bacteria through flow cytometry showed only a small decrease in FH binding after incubation of strain D39 with anti-PspC3 IgG, and one clinical isolate showed inhibition of sIgA binding by anti-PspC3 IgG. We conclude that although anti-PspC3 antibodies were able to recognize PspC variants from the majority of the strains tested, partial inhibition of FH and sIgA binding through anti-PspC3 antibodies in vitro could be observed for only a restricted number of isolates.

Item Type:	Article
Subjects:	QU Biochemistry > Genetics > QU 475 Genetic processes QU Biochemistry > Proteins. Amino Acids. Peptides > QU 58.5 DNA. QW Microbiology and Immunology > Antigens and Antibodies. Toxins and Antitoxins > QW 575 Antibodies QW Microbiology and Immunology > Immunotherapy and Hypersensitivity > QW 805 Vaccines. Antitoxins. Toxoids WC Communicable Diseases > Infection. Bacterial Infections > Bacterial Infections > WC 217 Pneumococcal infections
Faculty: Department:	Groups (2002 - 2012) > Clinical Group
Digital Object Identifer (DOI):	https://doi.org/10.1128/cvi.05706-11
Depositing User:	Lynn Roberts-Maloney
Date Deposited:	29 Jan 2015 14:39
Last Modified:	05 Nov 2019 14:56
URI:	https://archive.lstmed.ac.uk/id/eprint/4822

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