Oligopeptide permease in Borrelia burgdorferi:: putative peptide-binding components encoded by both chromosomal and plasmid loci

被引:95
作者
Bono, JL [1 ]
Tilly, K [1 ]
Stevenson, B [1 ]
Hogan, D [1 ]
Rosa, P [1 ]
机构
[1] NIAID, Rocky Mt Labs, Microbial Struct & Funct Lab, Hamilton, MT 59840 USA
来源
MICROBIOLOGY-UK | 1998年 / 144卷
关键词
oligopeptide permease; oppA; plasmids; Lyme disease; spirochaetes;
D O I
10.1099/00221287-144-4-1033
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
To elucidate the importance of oligopeptide permease for Borrelia burgdorferi, the agent of Lyme disease, a chromosomal locus in B. burgdorferi that encodes homologues of all five subunits of oligopeptide permease has been identified and characterized. B. burgdorferi has multiple copies of the gene encoding the peptide-binding component, OppA; three reside at the chromosomal locus and two are on plasmids. Northern analyses indicate that each oppA gene is independently transcribed, although the three chromosomal oppA genes are also expressed as bi-and tri-cistronic messages. Induction of one of the plasmid-encoded oppA genes was observed following an increase in temperature, which appears to be an important cue for adaptive responses in vivo. The deduced amino acid sequences suggest that all five borrelial OppA homologues are lipoproteins, but the protease-resistance of at least one of them in intact bacteria is inconsistent with outer-surface localization. Insertional inactivation of a plasmid-encoded oppA gene demonstrates that it is not essential for growth in culture.
引用
收藏
页码:1033 / 1044
页数:12
相关论文
共 54 条
  • [1] Tromp1, a putative rare outer membrane protein, is anchored by an uncleaved signal sequence to the Treponema pallidum cytoplasmic membrane
    Akins, DR
    Robinson, E
    Shevchenko, D
    Elkins, C
    Cox, DL
    Radolf, JD
    [J]. JOURNAL OF BACTERIOLOGY, 1997, 179 (16) : 5076 - 5086
  • [2] 3 HIGHLY HOMOLOGOUS MEMBRANE-BOUND LIPOPROTEINS PARTICIPATE IN OLIGOPEPTIDE TRANSPORT BY THE AMI SYSTEM OF THE GRAM-POSITIVE STREPTOCOCCUS-PNEUMONIAE
    ALLOING, G
    DEPHILIP, P
    CLAVERYS, JP
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1994, 241 (01) : 44 - 58
  • [3] ALTSCHUL SF, 1990, J MOL BIOL, V215, P403, DOI 10.1006/jmbi.1990.9999
  • [4] PHENOTYPIC REVERSAL IN DAM MUTANTS OF ESCHERICHIA-COLI K-12 BY A RECOMBINANT PLASMID CONTAINING THE DAM+ GENE
    ARRAJ, JA
    MARINUS, MG
    [J]. JOURNAL OF BACTERIOLOGY, 1983, 153 (01) : 562 - 565
  • [5] BARBOUR AG, 1984, YALE J BIOL MED, V57, P521
  • [6] VARIATION IN A MAJOR SURFACE PROTEIN OF LYME-DISEASE SPIROCHETES
    BARBOUR, AG
    TESSIER, SL
    HAYES, SF
    [J]. INFECTION AND IMMUNITY, 1984, 45 (01) : 94 - 100
  • [7] MOLECULAR ANALYSIS OF LINEAR PLASMID-ENCODED MAJOR SURFACE-PROTEINS, OSPA AND OSPB, OF THE LYME-DISEASE SPIROCHETE BORRELIA-BURGDORFERI
    BERGSTROM, S
    BUNDOC, VG
    BARBOUR, AG
    [J]. MOLECULAR MICROBIOLOGY, 1989, 3 (04) : 479 - 486
  • [8] LYME-DISEASE - A TICK-BORNE SPIROCHETOSIS
    BURGDORFER, W
    BARBOUR, AG
    HAYES, SF
    BENACH, JL
    GRUNWALDT, E
    DAVIS, JP
    [J]. SCIENCE, 1982, 216 (4552) : 1317 - 1319
  • [9] BACTERIAL SEX PHEROMONE-INDUCED PLASMID TRANSFER
    CLEWELL, DB
    [J]. CELL, 1993, 73 (01) : 9 - 12
  • [10] Characterization of a 30-kDa Borrelia burgdorferi substrate-binding protein homologue
    Das, S
    Shraga, D
    Gannon, C
    Lam, TT
    Feng, S
    Brunet, LR
    Telford, SR
    Barthold, SW
    Flavell, RA
    Fikrig, E
    [J]. RESEARCH IN MICROBIOLOGY, 1996, 147 (09) : 739 - 751