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2015 ; 83
(4
): 1339-46
Nephropedia Template TP
gab.com Text
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English Wikipedia
Type IV pilus glycosylation mediates resistance of Pseudomonas aeruginosa to
opsonic activities of the pulmonary surfactant protein A
#MMPMID25605768
Tan RM
; Kuang Z
; Hao Y
; Lee F
; Lee T
; Lee RJ
; Lau GW
Infect Immun
2015[Apr]; 83
(4
): 1339-46
PMID25605768
show ga
Pseudomonas aeruginosa is a major bacterial pathogen commonly associated with
chronic lung infections in cystic fibrosis (CF). Previously, we have demonstrated
that the type IV pilus (Tfp) of P. aeruginosa mediates resistance to
antibacterial effects of pulmonary surfactant protein A (SP-A). Interestingly, P.
aeruginosa strains with group I pilins are O-glycosylated through the TfpO
glycosyltransferase with a single subunit of O-antigen (O-ag). Importantly,
TfpO-mediated O-glycosylation is important for virulence in mouse lungs,
exemplified by more frequent lung infection in CF with TfpO-expressing P.
aeruginosa strains. However, the mechanism underlying the importance of Tfp
glycosylation in P. aeruginosa pathogenesis is not fully understood. Here, we
demonstrated one mechanism of increased fitness mediated by O-glycosylation of
group 1 pilins on Tfp in the P. aeruginosa clinical isolate 1244. Using an acute
pneumonia model in SP-A+/+ versus SP-A-/- mice, the O-glycosylation-deficient
?tfpO mutant was found to be attenuated in lung infection. Both 1244 and ?tfpO
strains showed equal levels of susceptibility to SP-A-mediated membrane
permeability. In contrast, the ?tfpO mutant was more susceptible to opsonization
by SP-A and by other pulmonary and circulating opsonins, SP-D and mannose binding
lectin 2, respectively. Importantly, the increased susceptibility to phagocytosis
was abrogated in the absence of opsonins. These results indicate that
O-glycosylation of Tfp with O-ag specifically confers resistance to opsonization
during host-mediated phagocytosis.