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Infection and Immunity, February 2000, p. 437-442, Vol. 68, No. 2
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Molecular Characterization of Mycoplasma arthritidis Membrane Lipoprotein MAA1

Leigh Rice Washburn,* Elizabeth J. Miller, and Keith E. Weaver

Division of Basic Biomedical Sciences, University of South Dakota, Vermillion, South Dakota 57069-2390

Received 14 June 1999/Returned for modification 24 August 1999/Accepted 8 November 1999

Genes encoding the Mycoplasma arthritidis surface-exposed lipoprotein MAA1 were cloned and sequenced from MAA1-expressing strains 158p10p9 and PG6, from a low-adherence (LA) variant derived from 158p10p9 that expresses a truncated version of MAA1 (MAA1Delta ) and from two MAA1-negative strains, 158 and H39. The deduced amino acid sequences of maa1 from 158p10p9 and PG6 predicted, respectively, 86.5- and 86.4-kDa basic, largely hydrophilic lipoproteins with 29-amino-acid signal peptides and predicted cleavage sites for signal peptidase II (Ala-Ala-Aladown-arrow Cys). The truncation in the LA variant resulted from a Gright-arrowT substitution at nucleotide 695, which created a premature stop codon. This, in turn, generated a predicted 26.6-kDa prolipoprotein (23.6 kDa after processing), consistent with an Mr of ~24,000 calculated for MAA1Delta . Similarly, absence of MAA1 expression in H39 and 158 resulted from Cright-arrowA substitutions at nucleotide 208, generating premature stop codons at that site in both strains.

* Corresponding author. Mailing address: Division of Basic Biomedical Sciences, University of South Dakota School of Medicine, Vermillion, SD 57069-2390. Phone: (605) 677-5170. Fax: (605) 677-5658. E-mail: lwashbur{at}usd.edu.

Infection and Immunity, February 2000, p. 437-442, Vol. 68, No. 2
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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