Molecular characterization of Mycoplasma arthritidis membrane lipoprotein MAA1

Citation
Lr. Washburn et al., Molecular characterization of Mycoplasma arthritidis membrane lipoprotein MAA1, INFEC IMMUN, 68(2), 2000, pp. 437-442
Citations number
19
Categorie Soggetti
Immunology
Journal title
INFECTION AND IMMUNITY
ISSN journal
00199567 → ACNP
Volume
68
Issue
2
Year of publication
2000
Pages
437 - 442
Database
ISI
SICI code
0019-9567(200002)68:2<437:MCOMAM>2.0.ZU;2-X
Abstract
Genes encoding the Mycoplasma arthritidis surface-exposed lipoprotein MAA1 were cloned and sequenced from MAA1-expressing strains 158p10p9 and PG6, fr om a low-adherence (LA) variant derived from 158p10p9 that expresses a trun cated version of MAA1 (MAA1 Delta) and from two MAA1-negative strains, 158 and H39, The deduced amino acid sequences of maa1 from 158p10p9 and PG6 pre dicted, respectively, 86.5- and 86.4-kDa basic, Largely hydrophilic lipopro teins with 29-amino-acid signal peptides and predicted cleavage sites for s ignal peptidase II (Ala-Ala-Ala down arrow Cys), The truncation in the LA v ariant resulted from a G-->T substitution at nucleotide 695, which created a premature stop codon, This, in turn, generated a predicted 26.6-kDa proli poprotein (23.6 kDa after processing), consistent with an M-r of similar to 24,000 calculated for MAA1 Delta. Similarly, absence of MAA1 expression in H39 and 158 resulted from C-->A substitutions at nucleotide 208, generatin g premature stop codons at that site in both strains.