Open AccessCharacterization of a major Mycoplasma penetrans lipoprotein and of its gene
Author(s) -
Ferris Stéphane,
L. Watson Harold,
Neyrolles Olivier,
Montagnier Luc,
Blanchard Alain
Publication year - 1995
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1995.tb07737.x
Subject(s) - gene , open reading frame , biology , signal peptide , gene product , oligonucleotide , peptide sequence , microbiology and biotechnology , sequence analysis , sequence (biology) , genetics , gene expression
A novel mycoplasmal species designated as Mycoplasma penetrans has been isolated recently from patients infected with human immunodeficiency virus. p35, a major antigen extracted from the membrane of this mycoplasma using Triton X‐114 has been found to be a lipoprotein. After proteolytic treatment of p35, the sequence of one of the resulting peptides was determined and a corresponding oligonucleotide was deduced. Using this oligonucleotide as a probe the p35 gene was cloned and sequenced. Sequence analysis revealed an amino‐terminal signal peptide with a potential acylation site which would result in a 35.3 kDa mature product. In addition, the p35 gene was followed by an open reading frame with a corresponding polypeptide partially homologous to p35, in particular to the N‐terminus region.