TY - JOUR
T1 - Oligopeptide permease in Borrelia burgdorferi
T2 - Putative peptide-binding components encoded by both chromosomal and plasmid loci
AU - Bono, James L.
AU - Tilly, Kit
AU - Stevenson, Brian
AU - Hogan, Dan
AU - Rosa, Patricia
PY - 1998/4
Y1 - 1998/4
N2 - 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.
AB - 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.
KW - Lyme disease
KW - Oligopeptide permease
KW - Plasmids
KW - Spirochaetes
KW - oppA
UR - http://www.scopus.com/inward/record.url?scp=0031967697&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0031967697&partnerID=8YFLogxK
U2 - 10.1099/00221287-144-4-1033
DO - 10.1099/00221287-144-4-1033
M3 - Article
C2 - 9579077
AN - SCOPUS:0031967697
SN - 1350-0872
VL - 144
SP - 1033
EP - 1044
JO - Microbiology
JF - Microbiology
IS - 4
ER -