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      SAPA/trans-sialidase and cruzipain: two antigens from Trypanosoma cruzi contain immunodominant but enzymatically inactive domains.

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          Abstract

          Trypanosoma cruzi, the parasitic protozoan that causes the American trypanosomiasis, or Chagas disease, contains a number of antigenic molecules, some of which have tandems of amino acid repeats. One of these molecules, SAPA (shed acute phase antigen), contains a so-far unique trans-sialidase activity that is essential for penetration of the parasite into mammalian cells. The enzyme consists of two different domains, one presumably enzymatic, which contains four copies of an amino acid motif conserved in bacterial neuraminidases, and the other highly antigenic, consisting of the repeats. Another enzyme that seems to be involved in the host-parasite relationship, the cysteine proteinase cruzipain, is also made up in its mature form of a catalytic domain with high homology to cathepsin L and a COOH-terminal domain that is highly antigenic in vivo. These bifunctional molecules may have arisen by incorporation of a highly antigenic domain to an essential enzyme in order to attract the immune response, thus protecting the enzyme activity.

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          Author and article information

          Journal
          FASEB J
          FASEB journal : official publication of the Federation of American Societies for Experimental Biology
          0892-6638
          0892-6638
          Nov 1992
          : 6
          : 14
          Affiliations
          [1 ] Instituto de Investigaciones Bioquimicas Fundacion Campomar, Buenos Aires, Argentina.
          Article
          1426764
          6cb16496-936b-48ef-a3d9-0b9d89568428
          History

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