Collagen degrading activity associated with Mycobacterium species.
BACKGROUND
The mechanism of Mycobacterium tuberculosis penetration into tissues is poorly understood but it is reasonable to assume that there is a contribution from proteases capable of disrupting the extracellular matrix of the pulmonary epithelium and the blood vessels. A study was undertaken to identify and characterise collagen degrading activity of M tuberculosis.


METHODS
Culture filtrate protein extract (CFPE) was obtained from reference mycobacterial strains and mycobacteria isolated from patients with tuberculosis. The collagen degrading activity of CFPE was determined according to the method of Johnson-Wint using 3H-type I collagen. The enzyme was identified by the Birkedal-Hansen and Taylor method and its molecular mass determined by SDS-PAGE and Sephacryl S-300 gel filtration chromatography using an electroelution purified enzyme.


RESULTS
CFPE from Mycobacterium tuberculosis strain H37Rv showed collagenolytic activity that was four times higher than that of the avirulent strain H37Ra. The 75 kDa enzyme responsible was divalent cation dependent. Other mycobacterial species and those isolated from patients with tuberculosis also had collagen degrading activity.


CONCLUSIONS
Mycobacterium species possess a metalloprotease with collagen degrading activity. The highest enzymatic activity was found in the virulent reference strain H37Rv.
Massó
F
F
Departamento de Biología Celular, Instituto Nacional de Cardiología "Ignacio Chávez", Juan Badiano 1, Tlalpan 14080, Mexico.
Paéz
A
A
Varela
E
E
de León
L D
LD
Zenteno
E
E
Montaño
L F
LF
D001431:Bacteriological Techniques; D003094:Collagen / Q000378:metabolism*; D006801:Humans; D008666:Metalloendopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D014376:Tuberculosis / Q000382:microbiology
D003094:Collagen; D008666:Metalloendopeptidases