CHARACTERIZATION OF THE ANTIGEN-85 COMPLEX FIBRONECTIN-BINDING PROTEINS DERIVED FROM AGED CULTURE FILTRATES OF MYCOBACTERIUM-BOVIS BCG, TICE(R) SUBSTRAIN
F. Oner et al., CHARACTERIZATION OF THE ANTIGEN-85 COMPLEX FIBRONECTIN-BINDING PROTEINS DERIVED FROM AGED CULTURE FILTRATES OF MYCOBACTERIUM-BOVIS BCG, TICE(R) SUBSTRAIN, Microbios, 78(315), 1994, pp. 69-81
The antigen 85 complex are major T-cell and B-cell antigens and fibron
ectin-binding proteins secreted by Mycobacterium tuberculosis, M. lepr
ae and attenuated M. bovis (BCG vaccine). The Ag 85 complex was found
to comprise a high proportion of the extracellular protein in filtrate
s of surface-pellicle cultures of Tice(R)-substrain BCG vaccine, attai
ning a maximum of 25%. This proportion began to decrease prior to the
end of the logarithmic growth phase, about 3 weeks after the start of
the culture, mainly due to apparent degradation of the Ag 85 complex.
Isolation of the main Ag 85 protein and determination of the first 36
residues of the NH2-terminus showed identity with the 85A protein isol
ated by others from various mycobacteria. Both the Ag 85A and B compon
ents were secreted in nearly constant proportions over a 6-week period
. No Ag 85C protein was detected.