Characterization of a major Mycoplasma penetrans lipoprotein and of its gene |
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Authors: | Sté phane Ferris,Harold L. Watson,Olivier Neyrolles,Luc Montagnier,Alain Blanchard |
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Affiliation: | Institut Pasteur, Departement du SIDA et des Retrovirus, Unitéd'Oncologie Virale et URA CNRS 1157, 28, rue du Dr. Roux, 75724 Paris Cedex 15, France |
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Abstract: | Abstract 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. |
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Keywords: | Mycoplasma penetrans
Lipoprotein/surface antigen Mollicute |
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