Chlamydia trachomatis OmcB protein is a surface-exposed glycosaminoglycan-dependent adhesin

被引:53
作者
Fadel, Sanaa [1 ]
Eley, Adrian [1 ]
机构
[1] Univ Sheffield, Sch Med, Div Genom Med, Henry Wellcome Labs Med Res, Sheffield S10 2RX, S Yorkshire, England
关键词
D O I
10.1099/jmm.0.46801-0
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The OmcB protein of Chlamydia trachomatis is a cysteine-rich outer membrane polypeptide with important functional, structural and antigenic properties. The entire gene encoding the OmcB protein from C. trachomatis serovar LGV1 was cloned and expressed in Escherichia coli and the full-length protein used to raise polyclonal antibodies. Recombinant OmcB was used to show that OmcB is a surface-exposed protein that functions as a chlamydial adhesin. Infectivity inhibition assays carried out using HeLa cells with serovar LGV1 in the presence of purified anti-OmcB serum showed inhibition of infectivity, suggesting that some of the OmcB was surface exposed. Moreover, using recombinant OmcB in infectivity inhibition assays resulted in 70% inhibition of infectivity, confirming that OmcB plays a role as an adhesin in C. trachomatis. Furthermore, recombinant OmcB protein bound to the surface of HeLa and Heel B cells, but binding to glycosaminoglycan (GAG)-deficient cells (pgsA-745 and pgsD-677) was markedly reduced, indicating that OmcB binds to GAG-like receptors on host cells.
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页码:15 / 22
页数:8
相关论文
共 41 条
[22]   Chlamydial infections in children [J].
Oroz, C ;
Porter-Boveri, KAM ;
Thompson, C .
SEXUALLY TRANSMITTED INFECTIONS, 2001, 77 (06) :462-462
[23]   DNA immunization followed by a viral vector booster in a Chlamydia pneumoniae mouse model [J].
Penttilä, T ;
Tammiruusu, A ;
Liljeström, P ;
Sarvas, M ;
Mäkelä, PH ;
Vuola, JM ;
Puolakkainen, M .
VACCINE, 2004, 22 (25-26) :3386-3394
[24]   Surface accessibility of the 70-kilodalton Chlamydia trachomatis heat shock protein following reduction of outer membrane protein disulfide bonds [J].
Raulston, JE ;
Davis, CH ;
Paul, TR ;
Hobbs, JD ;
Wyrick, P .
INFECTION AND IMMUNITY, 2002, 70 (02) :535-543
[25]  
Sambrook J., 1989, MOL CLONING LAB MANU, V2nd ed.
[26]  
SARDINIA LM, 1988, J GEN MICROBIOL, V134, P997
[27]   A SINGLE-STRAND SPECIFIC ENDONUCLEASE ACTIVITY COPURIFIES WITH OVEREXPRESSED T5 D15 EXONUCLEASE [J].
SAYERS, JR ;
ECKSTEIN, F .
NUCLEIC ACIDS RESEARCH, 1991, 19 (15) :4127-4132
[28]   comH, a novel gene essential for natural transformation of Helicobacter pylori [J].
Smeets, LC ;
Bijlsma, JJE ;
Boomkens, SY ;
Vandenbroucke-Grauls, CMJE ;
Kusters, JG .
JOURNAL OF BACTERIOLOGY, 2000, 182 (14) :3948-3954
[29]   Eukaryotic cell uptake of heparin-coated microspheres:: a model of host cell invasion by Chlamydia trachomatis [J].
Stephens, RS ;
Fawaz, FS ;
Kennedy, KA ;
Koshiyama, K ;
Nichols, B ;
van Ooij, C ;
Engel, JN .
INFECTION AND IMMUNITY, 2000, 68 (03) :1080-1085
[30]   Heparin-binding outer membrane protein of chlamydiae [J].
Stephens, RS ;
Koshiyama, K ;
Lewis, E ;
Kubo, A .
MOLECULAR MICROBIOLOGY, 2001, 40 (03) :691-699