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BIBTEX RIS

Localization of acetylated a-tubulin in Tritrichomonas foetus and Trichomonas vaginalis.

1988; Japan Society of Cell Biology; Volume: 13; Issue: 5 Linguagem: Inglês

10.1247/csf.13.445

1347-3700

Claudia Batista, Marlene Benchimol, Narcisa L. Cunha‐e‐Silva, Wanderley de Souza,

Cervical Cancer and HPV Research

We used monoclonal antibodies specific for acetylated and nonacetylated a-tubulin to detect and to localize microtubules containing acetylated a-tubulin (stable microtubules) in the pathogenic protozoa Tritrichomonas foetus and Trichomonas vaginalis. SDS-PAGE analysis showed that tubulin is amajor proteinof both parasites, being enriched in cytoskeletal preparations of whole cells extracted with Triton X-100. The monoclonal antibodies, which recognize all isoforms of a-tubulin (B-5-1-2) and only acetylated a-tubulin (6-11B-1), bind to the tubulin of T. foetus and T.vaginalis as seen by immunoblotting. Tubulin-containing structures were localized using immunofluorescence microscopy and transmission electron microscopy of the whole cytoskeleton previously incubated in the presence of the anti-tubulin antibodies and a second antibody-gold complex, and then processed using the negative staining or replica techniques. The results obtained indicate that, in addition to the flagellar microtubules, those which form the peltar-axostyle system represent stable microtubules containing acetylated alpha-tubulin.