The subtelomeric regions of the chromosomes of many organisms contain gene
families that allow adaptation to a changing environment. In a number of pa
rasites, these subtelomeric gene families encode cell surface proteins that
undergo antigenic variation. Proteases are another important virulence det
erminant in pathogenic microorganisms. We report the localization of the PR
T1 protease of the pathogenic fungus Pneumocystis carinii sp. f. carinii, e
ncoded by a subtelomeric gene family, to the cell surface of both the troph
ozoite and the cyst phase of the organism. Using anti-PRT1 antiserum, we de
monstrated specificity to P. carinii sp. f. carinii in sections of infected
rat lungs and, using immunofluorescence, we showed that the PRT1 protease
has the characteristic distribution of a surface protein. The anti-PRT1 ant
iserum showed cross-reactivity with a number of P. carinii sp. f, carinii p
roteins migrating between 185 kDa and 28 kDa, the majority migrating betwee
n 42 kDa and 52 kDa, a region that has been shown by serological studies to
contain important immunodominant P. carinii proteins. cross-reactivity was
also observed with P. carinii sp. f. hominis proteins. We have also cloned
a portion of the catalytic domain of PRT1 from P. carinii sp. f. hominis,
P, carinii sp. f. muris and P, carinii sp. f. rattus. Our data suggest that
the PRT1 protease plays an important role in the pathogenicity of P. carin
ii.