Characterization of a haemolysin from Mycobacterium tuberculosis with homology to a virulence factor of Serpulina hyodysenteriae

Scrutiny of sequence data from the Mycobacterium leprae genome sequencing project identified the presence of a gene encoding a 268-amino-acid polypeptide which is highly similar to a pore-forming haemolysin/cytotoxin virulence determinant, TlyA, from the swine pathogen Serpulina hyodysenteriae. Usin...

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Published in:	Microbiology (Society for General Microbiology) Vol. 144; no. 5; pp. 1205 - 1211
Main Authors:	Wren, B.W, Stabler, R.S, Das, S.S, Butcher, P.D, Mangan, J.A, Clarke, J.D, Casali, N, Parish, T, Stoker, N.G
Format:	Journal Article
Language:	English
Published:	Reading Soc General Microbiol 01-05-1998 Society for General Microbiology
Subjects:	Amino Acid Sequence animal health animal parasites and pests Animals arthropod pests Bacterial Proteins Bacteriology Biological and medical sciences Brachyspira hyodysenteriae - chemistry Brachyspira hyodysenteriae - genetics Brachyspira hyodysenteriae - pathogenicity Cloning, Molecular Fundamental and applied biological sciences. Psychology genbank/x98295 Genes, Bacterial Genetics Hemolysin Proteins - chemistry Hemolysin Proteins - genetics Hemolysin Proteins - metabolism Hemolysis human health and safety Humans medicine Microbiology Molecular Sequence Data Mycobacterium - chemistry Mycobacterium - genetics Mycobacterium leprae Mycobacterium tuberculosis Mycobacterium tuberculosis - chemistry Mycobacterium tuberculosis - genetics Polymerase Chain Reaction Sequence Analysis, DNA Sequence Homology, Amino Acid Serpulina hyodysenteriae Species Specificity Transcription, Genetic Virulence - genetics Toxin Mycobacterium tuberculosis Nucleotide sequence Mycobacteriales Mycobacteriaceae Bacteria Homology Actinomycetes Gene expression Hemolysin Biological activity Aminoacid sequence
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Summary:	Scrutiny of sequence data from the Mycobacterium leprae genome sequencing project identified the presence of a gene encoding a 268-amino-acid polypeptide which is highly similar to a pore-forming haemolysin/cytotoxin virulence determinant, TlyA, from the swine pathogen Serpulina hyodysenteriae. Using degenerate oligonucleotide primers based on the TlyA sequences, the Mycobacterium tuberculosis homologue was amplified and this product was used to obtain the clone and sequence a 2.5 kb fragment containing the whole M. tuberculosis tlyA gene. tlyA encodes a 267-amino-acid protein with a predicted molecular mass of 28 kDa. TlyA homologues were identified by PCR in M. leprae, Mycobacterium avium and Mycobacterium bovis BCG, but appeared absent in Mycobacterium smegmatis, Mycobacterium vaccae, Mycobacterium kansasii, Mycobacterium chelonae and Mycobacterium phlei. The M. tuberculosis gene appeared to be the first gene in an operon containing at least two other genes. Introduction of the M. tuberculosis tlyA gene into M. smegmatis using a mycobacterial shuttle expression plasmid converted non-haemolytic cells into those exhibiting significant haemolytic activity. Similarly, inducible haemolytic activity was observed in sonicated bacteria when tlyA was expressed as a His6-tagged fusion protein in Escherichia coli. tlyA mRNA was detected in both M. tuberculosis and M. bovis BCG using RT-PCR, confirming that this gene is expressed in organisms cultured in vitro.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1350-0872 1465-2080
DOI:	10.1099/00221287-144-5-1205