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2016 ; 196
(1
): 385-94
Nephropedia Template TP
gab.com Text
Twit Text FOAVip
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English Wikipedia
The Group B Streptococcus-Secreted Protein CIP Interacts with C4, Preventing C3b
Deposition via the Lectin and Classical Complement Pathways
#MMPMID26608922
Pietrocola G
; Rindi S
; Rosini R
; Buccato S
; Speziale P
; Margarit I
J Immunol
2016[Jan]; 196
(1
): 385-94
PMID26608922
show ga
The group B Streptococcus (GBS) is a leading cause of neonatal invasive disease.
GBS bacteria are surrounded by a thick capsular polysaccharide that is a potent
inhibitor of complement deposition via the alternative pathway. Several of its
surface molecules can however activate the classical and lectin complement
pathways, rendering this species still vulnerable to phagocytic killing. In this
study we have identified a novel secreted protein named complement interfering
protein (CIP) that downregulates complement activation via the classical and
lectin pathways, but not the alternative pathway. The CIP protein showed high
affinity toward C4b and inhibited its interaction with C2, presumably preventing
the formation of the C4bC2a convertase. Addition of recombinant CIP to GBS
cip-negative bacteria resulted in decreased deposition of C3b on their surface
and in diminished phagocytic killing in a whole-blood assay. Our data reveal a
novel strategy exploited by GBS to counteract innate immunity and could be
valuable for the development of anti-infective agents against this important
pathogen.