Oligopeptide permease in Borrelia burgdorferi: putative peptide-binding components encoded by both chromosomal and plasmid loci
- 1 April 1998
- journal article
- Published by Microbiology Society in Microbiology
- Vol. 144 (4), 1033-1044
- https://doi.org/10.1099/00221287-144-4-1033
Abstract
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.Keywords
This publication has 48 references indexed in Scilit:
- Tromp1, a putative rare outer membrane protein, is anchored by an uncleaved signal sequence to the Treponema pallidum cytoplasmic membraneJournal of Bacteriology, 1997
- Characterization of a 30-kDa Borrelia burgdorferi substrate-binding protein homologueResearch in Microbiology, 1996
- Three Highly Homologous Membrane-bound Lipoproteins Participate in Oligopeptide Transport by the Ami System of the Gram-positive Streptococcus pneumoniaeJournal of Molecular Biology, 1994
- Bacterial sex pheromone-induced plasmid transferCell, 1993
- ABC Transporters: From Microorganisms to ManAnnual Review of Cell Biology, 1992
- Elimination of Borrelia burgdorferi from vector ticks feeding on OspA-immunized mice.Proceedings of the National Academy of Sciences, 1992
- Molecular analysis of linear plasmid‐encoded major surface proteins, OspA and OspB, of the Lyme disease spirochaete Borrelia burgdorferiMolecular Microbiology, 1989
- Uptake of cell wall peptides by Salmonella typhimurium and Escherichia coliJournal of Bacteriology, 1987
- A family of related ATP-binding subunits coupled to many distinct biological processes in bacteriaNature, 1986
- Lyme Disease—a Tick-Borne Spirochetosis?Science, 1982