Document Detail

Mycobacterium smegmatis produces an HBHA homologue which is not involved in epithelial adherence.
MedLine Citation:
PMID:  17208488     Owner:  NLM     Status:  MEDLINE    
Mycobacterium tuberculosis produces heparin-binding hemagglutinin (TB-HBHA), an adhesin involved in binding to non-professional phagocytes and in extrapulmonary dissemination. TB-HBHA binds sulphated glycoconjugates through its C-terminal lysine-rich domain and can be purified by heparin-Sepharose chromatography. Homologues of HBHA are found in other pathogenic mycobacteria, but previous investigations failed to demonstrate them in non-pathogenic Mycobacterium smegmatis. We identified a gene encoding a HBHA-like protein, named MS-HBHA, from the complete M. smegmatis genome. The deduced MS-HBHA amino acid sequence revealed 68% identity with that of TB-HBHA and contains lysine-rich repeats in its C-terminal domain. However, in contrast to TB-HBHA, the lysine-rich domain of MS-HBHA is preceded by a stretch of acidic residues. This difference likely explains the low affinity for heparin displayed by MS-HBHA compared to TB-HBHA. Isolation by heparin-Sepharose chromatography procedure and mass spectrometry analysis indicated that MS-HBHA, similar to TB-HBHA contains several methylated lysine residues in its C-terminal domain. Although MS-HBHA is associated with M. smegmatis cell wall fractions, it does not seem to play a role in epithelial adherence and its function remains unknown. We therefore conclude that TB-HBHA may have evolved as an adhesin in pathogenic mycobacteria from a homolog that serves a different function in a saprophytic mycobacterium.
Franck Biet; Maria Angela de Melo Marques; Maggy Grayon; Erika Kopp Xavier da Silveira; Patrick J Brennan; Hervé Drobecq; Dominique Raze; Maria Cristina Vidal Pessolani; Camille Locht; Franco Dante Menozzi
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Publication Detail:
Type:  Journal Article     Date:  2006-12-12
Journal Detail:
Title:  Microbes and infection / Institut Pasteur     Volume:  9     ISSN:  1286-4579     ISO Abbreviation:  Microbes Infect.     Publication Date:  2007 Feb 
Date Detail:
Created Date:  2007-02-16     Completed Date:  2007-08-17     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100883508     Medline TA:  Microbes Infect     Country:  France    
Other Details:
Languages:  eng     Pagination:  175-82     Citation Subset:  IM    
UR1282, Infectiologie Animale, Santé Publique (IASP-311), INRA Centre de Tours, F-37380 Nouzilly France.
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MeSH Terms
Adhesins, Bacterial / biosynthesis*,  genetics,  isolation & purification
Amino Acid Sequence
Bacterial Adhesion*
Bacterial Proteins / biosynthesis*,  genetics,  isolation & purification
Cell Fractionation
Cell Line
Cell Wall / chemistry
DNA, Bacterial / chemistry,  genetics
Epithelial Cells / microbiology*
Genome, Bacterial / genetics
Lectins / biosynthesis*,  genetics,  isolation & purification
Mass Spectrometry
Molecular Sequence Data
Mycobacterium smegmatis / genetics,  physiology*
Protein Structure, Tertiary / genetics
Repetitive Sequences, Amino Acid / genetics
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Reg. No./Substance:
0/Adhesins, Bacterial; 0/Bacterial Proteins; 0/DNA, Bacterial; 0/Lectins; 0/heparin-binding hemagglutinin

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