L-ficolin/mannose-binding lectin-associated serine protease complexes bind to group B streptococci primarily through N-acetylneuraminic acid of capsular polysaccharide and activate the complement pathway.

L-ficolin/mannose-binding lectin-associated serine protease complexes bind to group B streptococci primarily through N-acetylneuraminic acid of capsular polysaccharide and activate the complement pathway. Research Abstract Details 

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L-ficolin/mannose-binding lectin-associated serine protease complexes bind to group B streptococci primarily through N-acetylneuraminic acid of capsular polysaccharide and activate the complement pathway. Abstract Text:

Youko Aoyagi,Elisabeth E Adderson,Craig E Rubens,John F Bohnsack,Jin G Min,Misao Matsushita,Teizo Fujita,Yoshiyuki Okuwaki,Shinji Takahashi,Youko Aoyagi,Elisabeth E Adderson,Craig E Rubens,John F Bohnsack,Jin G Min,Misao Matsushita,Teizo Fujita,Yoshiyuki Okuwaki,Shinji Takahashi,Youko Aoyagi,Elisabeth E Adderson,Craig E Rubens,John F Bohnsack,Jin G Min,Misao Matsushita,Teizo Fujita,Yoshiyuki Okuwaki,Shinji Takahashi,

Group B streptococci (GBS) are the most common cause of neonatal sepsis and meningitis. Most infants who are colonized with GBS at birth do not develop invasive disease, although many of these uninfected infants lack protective levels of capsular polysaccharide (CPS)-specific antibody. The lectin pathway of complement is a potential mechanism for initiating opsonization of GBS with CPS-specific antibody-deficient serum. In this study, we determined whether mannose-binding lectin (MBL)/MBL-associated serine protease (MASP) complexes and L-ficolin/MASP complexes bind to different strains of GBS to activate the lectin pathway, and we identified the molecules recognized by lectins on the GBS surface. We found that MBL did not bind to any GBS examined, whereas L-ficolin bound to GBS cells of many serotypes. L-ficolin binding to GBS cells correlated with the CPS content in serotypes Ib, III (restriction digestion pattern types III-2 and III-3), and V but not with the group B-specific polysaccharide (GBPS) content or with the lipoteichoic acid (LTA) content. L-ficolin bound to purified CPS and GBPS in a concentration-dependent manner but not to purified LTA. All strains to which L-ficolin/MASP complexes bound consumed C4. When N-acetylneuraminic acid (NeuNAc) was selectively removed from GBS cells by treatment with neuraminidase, the reduction in L-ficolin binding was correlated with the amount of NeuNAc removed. Additionally, L-ficolin was able to bind to wild-type strains but was able to bind only weakly to unencapsulated mutants and a mutant strain in which the CPS lacks NeuNAc. We concluded that L-ficolin/MASP complexes bind to GBS primarily through an interaction with NeuNAc of CPS.

L-ficolin/mannose-binding lectin-associated serine protease complexes bind to group B streptococci primarily through N-acetylneuraminic acid of capsular polysaccharide and activate the complement pathway. Publishing Authors By Initials

Y Aoyagi,EE Adderson,CE Rubens,JF Bohnsack,JG Min,M Matsushita,T Fujita,Y Okuwaki,S Takahashi,Y Aoyagi,EE Adderson,CE Rubens,JF Bohnsack,JG Min,M Matsushita,T Fujita,Y Okuwaki,S Takahashi,Y Aoyagi,EE Adderson,CE Rubens,JF Bohnsack,JG Min,M Matsushita,T Fujita,Y Okuwaki,S Takahashi,

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L-ficolin/mannose-binding lectin-associated serine protease complexes bind to group B streptococci primarily through N-acetylneuraminic acid of capsular polysaccharide and activate the complement pathway. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Infection and immunity

VOLUME: 76

Page Numbers: 179-88

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ISSN: 1098-5522

DAY: 15

MONTH: 10

YEAR: 2007

L-ficolin/mannose-binding lectin-associated serine protease complexes bind to group B streptococci primarily through N-acetylneuraminic acid of capsular polysaccharide and activate the complement pathway. Information

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LANGUAGE: eng

NlmUniqueID: 246127

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AFFILIATION: Division of Microbiology, Joshi-Eiyoh University, Sakado, Saitama 350-0288, Japan.

Country: United States

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MEDLINETA: Infect Immun

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