3 DIFFERENT PUTATIVE PHOSPHATE-TRANSPORT RECEPTORS ARE ENCODED BY THEMYCOBACTERIUM-TUBERCULOSIS GENOME AND ARE PRESENT AT THE SURFACE OF MYCOBACTERIUM-BOVIS BCG
P. Lefevre et al., 3 DIFFERENT PUTATIVE PHOSPHATE-TRANSPORT RECEPTORS ARE ENCODED BY THEMYCOBACTERIUM-TUBERCULOSIS GENOME AND ARE PRESENT AT THE SURFACE OF MYCOBACTERIUM-BOVIS BCG, Journal of bacteriology, 179(9), 1997, pp. 2900-2906
A gene encoding a protein homologous to the periplasmic ARC phosphate
binding receptor PstS from Escherichia coli was cloned and sequenced f
rom a lambda gt11 library of Mycobacterium tuberculosis by screening w
ith monoclonal antibody 2A1-2, Its degree of similarity to the E. coli
PstS is comparable to those of the previously described dl, tuberculo
sis phosphate binding protein pab (Ag78, Ag5, or 38-kDa protein) and a
nother M. tuberculosis protein which we identified recently, We sugges
t that the three nl. tuberculosis proteins share a similar function an
d could be named PstS-1, PstS-2, and PstS-3, respectively, Molecular m
odeling of their three-dimensional structures using the structure of t
he E. coli PstS as a template and their inducibility by phosphate star
vation support this view., Recombinant PstS-2 and PstS-3 were produced
and purified by affinity chromatography. With PstS-1, these proteins
were used to demonstrate the specificity of three groups of monoclonal
antibodies. Using these antibodies in flow cytometry and immunoblotti
ng analyses, me demonstrate that the three genes are expressed and the
ir protein products are present and accessible at tile mycobacterial s
urface as well as in its culture filtrate, Together with the M. tuberc
ulosis genes encoding homologs of the PstA, PstB, and PstC components
we cloned before, the present data suggest that at least one, and poss
ibly several, related and functional ABC phosphate transporters exist
in mycobacteria. It, is hypothesized that the mycobacterial gene dupli
cations presented here may be a subtle adaptation of intracellular pat
hogens to phosphate starvation in their alternating growth environment
s.