Pilus backbone protein PitB of Streptococcus pneumoniae contains stabilizing intramolecular isopeptide bonds

被引：4

作者：

Zaehner, Dorothea ^{[1
,4
]}

Gandhi, Ashish R. ^{[1
]}

Stuchlik, Olga ^{[3
]}

Reed, Matthew ^{[3
]}

Pohl, Jan ^{[3
]}

Stephens, David S. ^{[1
,2
,4
]}

机构：

[1] Emory Univ, Sch Med, Dept Med, Div Infect Dis, Atlanta, GA 30322 USA

[2] Emory Univ, Sch Med, Rollins Res Ctr, Dept Microbiol & Immunol, Atlanta, GA 30322 USA

[3] Ctr Dis Control & Prevent, Biotechnol Core Facil Branch, Atlanta, GA 30329 USA

[4] Dept Vet Affairs Med Ctr Atlanta, Decatur, GA 30033 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2011年 / 409卷 / 03期

关键词：

Fimbrial protein; Intramolecular cross-link; Proteolytic stability; Thermal stability; Mass spectrometry; CORYNEBACTERIUM-DIPHTHERIAE; SURFACE PROTEIN; CELL-WALL; PYOGENES; ADHESION; LINKAGE; REGION; DOMAIN; M3;

D O I：

10.1016/j.bbrc.2011.05.038

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Streptococcus pneumoniae type 2 pili are recently identified fimbrial structures extending from the bacterial surface and formed by polymers of the structural protein PitB. Intramolecular isopeptide bonds are a characteristic of the related pilus backbone protein Spy0128 of group A streptococci. Based on the identification of conserved residues in PitB, we predicted two intramolecular isopeptide bonds in PitB. Using a combination of tandem mass spectrometry and Edman sequencing, we show that these bonds were formed between Lys(63)-Asn(214) and Lys(243)-Asn(372) in PitB. Mutant proteins lacking the intramolecular isopeptide bonds retained the proteolytic stability observed with the wild type protein. However, absence of these bonds substantially decreased the melting temperature of the PitB-derivatives, indicating a stabilizing function of these bonds in PitB of the pneumococcal type 2 pilus. (C) 2011 Elsevier Inc. All rights reserved.

引用

页码：526 / 531

页数：6

共 25 条

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