Pathogenic Neisseria Bind the Complement Protein CFHR5 via Outer Membrane Porins.

Autor:	Yee WX; Sir William Dunn School of Pathology, University of Oxfordgrid.4991.5, Oxford, United Kingdom., Tang CM; Sir William Dunn School of Pathology, University of Oxfordgrid.4991.5, Oxford, United Kingdom., Lavender H; Sir William Dunn School of Pathology, University of Oxfordgrid.4991.5, Oxford, United Kingdom.
Jazyk:	angličtina
Zdroj:	Infection and immunity [Infect Immun] 2022 Oct 20; Vol. 90 (10), pp. e0037722. Date of Electronic Publication: 2022 Oct 04.
DOI:	10.1128/iai.00377-22
Abstrakt:	Neisseria meningitidis and Neisseria gonorrhoeae are important human pathogens that have evolved to bind the major negative regulator of the complement system, complement factor H (CFH). However, little is known about the interaction of pathogens with CFH-related proteins (CFHRs) which are structurally similar to CFH but lack the main complement regulatory domains found in CFH. Insights into the role of CFHRs have been hampered by a lack of specific reagents. We generated a panel of CFHR-specific monoclonal antibodies and demonstrated that CFHR5 was bound by both pathogenic Neisseria spp. We showed that CFHR5 bound to PorB expressed by both pathogens in the presence of sialylated lipopolysaccharide and enhanced complement activation on the surface of N. gonorrhoeae. Our study furthered our understanding of the interactions of CFHRs with bacterial pathogens and revealed that CFHR5 bound the meningococcus and gonococcus via similar mechanisms.
Databáze:	MEDLINE
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