Influence of proteins Bsp and FemH on cell shape and peptidoglycan composition in group B streptococcus

被引:23
作者
Reinscheid, DJ [1 ]
Stosser, C
Ehlert, K
Jack, RW
Möller, K
Eikmanns, BJ
Chhatwal, GS
机构
[1] Univ Ulm, Dept Microbiol & Biotechnol, D-89069 Ulm, Germany
[2] GBF, Dept Microbiol, Natl Res Ctr Biotechnol, D-38124 Braunschweig, Germany
[3] Bayer AG, PH Res Anitiinfectives 1, D-42096 Wuppertal, Germany
[4] Univ Tubingen, Inst Organ Chem, D-72070 Tubingen, Germany
来源
MICROBIOLOGY-SGM | 2002年 / 148卷
关键词
Streptococcus agalactiae; murein hydrolase; fem-like genes;
D O I
10.1099/00221287-148-10-3245
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Group B streptococcus (GBS) is surrounded by a capsule. However, little is known about peptidoglycan metabolism in these bacteria. In the present study, a 65 kDa protein was isolated from the culture supernatant of GBS and N-terminally sequenced, permitting isolation of the corresponding gene, termed bsp. The bsp gene was located close to another gene, designated femH, and reverse transcription-PCR revealed a bicistronic transcriptional organization for both genes. The Bsp protein was detected in the culture supernatant from 31 tested clinical isolates of GBS, suggesting a wide distribution of Bsp in these bacteria. Overexpression of bsp resulted in lens-shaped GBS cells, indicating a role for bsp in controlling cell morphology. Insertional disruption of femH resulted in a reduction of the L-alanine content of the peptidoglycan, suggesting that femH is involved in the incorporation of L-alanine residues in the interpeptide chain of the peptidoglycan of GBS.
引用
收藏
页码:3245 / 3254
页数:10
相关论文
共 51 条
[1]  
Baker C.J., 1995, INFECT DIS FETUS NEW, V37, P980
[2]  
Beatson SA, 1998, FEMS MICROBIOL LETT, V163, P73
[3]   Self-protection against cell wall hydrolysis in Streptococcus milleri NMSCC 061 and analysis of the millericin B operon [J].
Beukes, M ;
Hastings, JW .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2001, 67 (09) :3888-3896
[4]   GUANIDINE EXTRACTION ENHANCES THE BINDING OF HUMAN-FIBRINOGEN TO GROUP-B STREPTOCOCCI [J].
CHHATWAL, GS ;
LAMMLER, C ;
BLOBEL, H .
MEDICAL MICROBIOLOGY AND IMMUNOLOGY, 1984, 173 (01) :19-27
[5]   A 60-kilodalton immunodominant glycoprotein is essential for cell wall integrity and the maintenance of cell shape in Streptococcus mutans [J].
Chia, JS ;
Chang, LY ;
Shun, CT ;
Chang, YY ;
Chen, JY .
INFECTION AND IMMUNITY, 2001, 69 (11) :6987-6998
[6]   ABNORMAL PEPTIDOGLYCAN PRODUCED IN A METHICILLIN-RESISTANT STRAIN OF STAPHYLOCOCCUS-AUREUS GROWN IN THE PRESENCE OF METHICILLIN - FUNCTIONAL-ROLE FOR PENICILLIN-BINDING PROTEIN-2A IN CELL-WALL SYNTHESIS [J].
DEJONGE, BLM ;
TOMASZ, A .
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 1993, 37 (02) :342-346
[7]   CONTROLLING BASAL EXPRESSION IN AN INDUCIBLE T7 EXPRESSION SYSTEM BY BLOCKING THE TARGET T7 PROMOTER WITH LAC REPRESSOR [J].
DUBENDORFF, JW ;
STUDIER, FW .
JOURNAL OF MOLECULAR BIOLOGY, 1991, 219 (01) :45-59
[8]   Site-specific serine incorporation by Lif and Epr into positions 3 and 5 of the staphylococcal peptidoglycan interpeptide bridge [J].
Ehlert, K ;
Tschierske, M ;
Mori, C ;
Schröder, W ;
Berger-Bächi, B .
JOURNAL OF BACTERIOLOGY, 2000, 182 (09) :2635-2638
[9]   Antimicrobial susceptibilities of group B streptococci isolated between 1992 and 1996 from patients with bacteremia or meningitis [J].
Fernandez, M ;
Hickman, ME ;
Baker, CJ .
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 1998, 42 (06) :1517-1519
[10]  
Filipe SR, 2000, J BIOL CHEM, V275, P27768