A murine monoclonal antibody (83L-2D3/a) to a dominant surface antigen of Leishmania braziliensis panamensis (WRAIR-470) recognized a determinant expressed on the surface membrane of mouse peritoneal macrophages infected in vitro. This determinant, also demonstrable on the surface membrane of intracellular amastigotes, was not displayed by the macrophage until at least 6 hr post-infection. This delay in expression and the obvious negativity of all uninfected macrophages inherent to infected cultures implied that the leishmania determinant had an intracellular origin. Furthermore, expression was dependent upon maintenance of macrophage function. When the parasite burden became overwhelming, additional antigen processing ceased, and that which had accumulated was either shed into the medium or was internalized. Immunochemical analyses revealed that the 83L-2D3/a reactive epitope was part of a 15,000 dalton molecule, which in all likelihood represents a breakdown product of a major surface glycoconjugate that had been degraded in the phagolysosome.

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