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    Defining targets for complement components C4b and C3b on the pathogenic neisseriae

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    Authors
    Lewis, Lisa A.
    Ram, Sanjay
    Prasad, Alpana
    Gulati, Sunita
    Getzlaff, Silke
    Blom, Anna M.
    Vogel, Ulrich
    Rice, Peter A.
    UMass Chan Affiliations
    Division of Infectious Diseases and Immunology
    Document Type
    Journal Article
    Publication Date
    2007-11-07
    Keywords
    Bacterial Outer Membrane Proteins
    Complement C3b
    Complement C4b
    Humans
    Neisseria gonorrhoeae
    Neisseria meningitidis
    Porins
    Protein Binding
    Protein Isoforms
    Life Sciences
    Medicine and Health Sciences
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    Abstract
    Complement is a key arm of the innate immune defenses against the pathogenic neisseriae. We previously identified lipooligosaccharide on Neisseria meningitidis as an acceptor for complement C4b. Little is known about other neisserial targets for complement proteins C3 and C4, which covalently attach to bacterial surfaces and initiate opsonization and killing. In this study we demonstrate that Neisseria gonorrhoeae porin (Por) 1B selectively binds C4b via amide linkages and C3b via ester linkages. Using strains expressing hybrid Por1A/1B molecules, a region spanned by loops 4 and 5 of Por1B was identified as the preferred binding site for C4b. We also identified the opacity protein (Opa), a major adhesin of pathogenic neisseriae, as a target for C4b and C3b on both N. meningitidis and N. gonorrhoeae. Using N. gonorrhoeae variants that predominantly expressed individual Opa proteins, we found that all Opa proteins tested (A, B, C, D, E, F, and I) bound C4b and C3b via amide and ester linkages, respectively. Amide linkages with Por1B and Opa were confirmed using serum containing only the C4A isoform, which exclusively forms amide linkages with targets. While monomers and heterodimers of C4Ab were detected on bacterial targets, C4Bb appeared to preferentially participate in heterodimer (C5 convertase) formation. Our data provide another explanation for the enhanced serum sensitivity of Por1B-bearing gonococci. The binding of C3b and C4b to Opa provides a rationale for the recovery of predominantly "transparent" (Opa-negative) neisserial isolates from persons with invasive disease, where the bacteria encounter high levels of complement.
    Source
    Infect Immun. 2008 Jan;76(1):339-50. Epub 2007 Nov 5. Link to article on publisher's site
    DOI
    10.1128/IAI.00613-07
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/38397
    PubMed ID
    17984207
    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1128/IAI.00613-07
    Scopus Count
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    UMass Chan Faculty and Researcher Publications

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