Advertisement
Journal Articles
Gene deletion suggests a role for Trypanosoma cruzi surface glycoprotein GP72 in the insect and mammalian stages of the life cycle
A.R. de Jesus, R. Cooper, M. Espinosa, J.E. Gomes, E.S. Garcia, S. Paul, G.A. Cross
Journal of Cell Science 1993 106: 1023-1033;

Summary

We have explored the biological function of a surface glycoprotein (GP72) of Trypanosoma cruzi by studying a null mutant parasite, generated by targeted gene deletion. GP72 deletion affected parasite morphology in several stages of the life cycle. Insect midgut (epimastigote) forms had a detached flagellum (apomastigote) in the null mutant. The abnormal flagellar phenotype persisted during development of the infective (metacyclic) forms but there was no impairment in the acquisition of complement resistance, sialidase expression or cell infectivity. The GP72 null mutant could efficiently infect and proliferate in mouse macrophages and non-phagocytic L6E9 cells. The mammalian stages of the life cycle also showed major morphological abnormalities. During early subcultures in L6E9 cells, few extracellular fully flagellated forms, expressing markers characteristic of trypomastigotes, were seen. The extracellular population consisted almost exclusively of rounded forms with short flagella (micromastigote), which expressed an amastigote-specific surface marker and no sialidase. The propagation of the parasite was not affected, despite the apparent lack of the trypomastigote forms, which are thought to be primarily responsible for cell invasion. After some subcultures, the extracellular population changed to about equal numbers of micromastigotes and a range of flagellated forms that still did not include true trypomastigotes. Instead, the kinetoplast remained close to the nucleus and the flagellum emerged from the middle of the cell (mesomastigote). Half of the flagellum adhered to the cell body and the remainder was free at the anterior end. In Triatoma infestans, the survival of the mutant was dramatically reduced, suggesting that either GP72 itself, or the altered properties of the flagellum, were critical for establishment in the insect vector.

REFERENCES

    1. Andrews N. W.,
    2. Hong K. S.,
    3. Robbins E. S. and
    4. Nussenzweig V.
    (1987). Stage-specific surface antigens expressed during the morphogenesis of vertebrate forms of Trypanosoma cruzi. Exp. Parasitol 64, 474–484
    OpenUrlCrossRefPubMedWeb of Science
    1. Chapman M. D.,
    2. Snary D. and
    3. Miles M. A.
    (1984). Quantitative differences in the expression of a 72,000 molecular weight cell glycoprotein (GP72) in T. cruzi zymodemes. J. Immunol 132, 3149–3153
    OpenUrlAbstract
    1. Cooper R.,
    2. Inverso J. A.,
    3. Espinosa M.,
    4. Nogueira N. and
    5. Cross G. A. M.
    (1991). Characterization of a candidate gene for GP72, an insect stage-specific antigen of Trypanosoma cruzi. Mol. Biochem. Parasitol 49, 45–60
    OpenUrlCrossRefPubMedWeb of Science
    1. Cooper R.,
    2. Ribeiro de Jesus A. and
    3. Cross G. A. M.
    (1993). Deletion of an immunodominant Trypanosoma cruzi surface glycoprotein disrupts flagellum-cell adhesion. J. Cell Biol 122, 149–156
    OpenUrlAbstract/FREE Full Text
    1. Cross G. A. M. and
    2. Takle G.
    (1993). The surface trans -sialidase family of Trypanosoma cruzi. Annu. Rev. Microbiol 46, 385–411
    OpenUrlCrossRef
    1. Ferguson M. A. J.,
    2. Allen A. K. and
    3. Snary D.
    (1983). Studies on the structure of a phosphoglycoprotein from the parasitic protozoan Trypanosoma cruzi. Biochem. J 213, 313–319
    OpenUrlAbstract/FREE Full Text
    1. Harth G.,
    2. Mills A. A.,
    3. Souto-Padron T. and
    4. Souza W.
    (1992). Trypanosoma cruzi glycoprotein 72: immunological analysis and cellular localization. Mol. Cell. Biochem 109, 25–36
    OpenUrlCrossRefPubMed
    1. Kirchhoff L. V.,
    2. Hieny S.,
    3. Shiver M. G.,
    4. Snary D. and
    5. Sher A.
    (1984). Cryptic epitope explains the failure of a monoclonal antibody to bind to certain isolates of Trypanosoma cruzi. J. Immunol 133, 2731–2735
    OpenUrlAbstract
    1. Nogueira N.,
    2. Chaplan S.,
    3. Tydings J. D.,
    4. Unkeless J. and
    5. Cohn Z.
    (1981). Trypanosoma cruzi: Surface antigens of blood and culture forms. J. Exp. Med 153, 629–639
    OpenUrlAbstract/FREE Full Text
    1. Nogueira N.,
    2. Unkeless J. and
    3. Cohn Z.
    (1982). Specific glycoprotein antigens on the surface of insect and mammalian stages of Trypanosoma cruzi. Proc. Nat. Acad. Sci. USA 79, 1259–1263
    OpenUrlAbstract/FREE Full Text
    1. Pereira M. E. A.
    (1983). A developmentally regulated neuraminidase activity in Trypanosoma cruzi. Science 219, 1444–1446
    OpenUrlAbstract/FREE Full Text
    1. Pimenta P. F. P.,
    2. Turco S. J.,
    3. McConville M. J.,
    4. Lawyer P. G.,
    5. Perkins P. V. and
    6. Sacks D. L.
    (1992). Stage-specific adhesion of Leishmania promastigotes to the sandfly midgut. Science 256, 1812–1815
    OpenUrlAbstract/FREE Full Text
    1. Robinson D. R. and
    2. Gull K.
    (1991). Basal body movements as a mechanism for mitochondrial genome segregation in the trypanosome cell cycle. Nature 352, 731–733
    OpenUrlCrossRefPubMedWeb of Science
    1. Schenkman S.,
    2. Carvalho L. P. and
    3. Nussenzweig V.
    (1992). Trypanosoma cruzi trans-sialidase and neuraminidase activities can be mediated by the same enzymes. J. Exp. Med 175, 567–575
    OpenUrlAbstract/FREE Full Text
    1. Sher A. and
    2. Snary D.
    (1982). Specific inhibition of the morphogenesis of Trypanosoma cruzi by a monoclonal antibody. Nature 300, 639–640
    OpenUrlCrossRefPubMed
    1. Snary D.,
    2. Ferguson M. A. J.,
    3. Scott M. T. and
    4. Allen A. K.
    (1981). Cell surface antigens of Trypanosoma cruzi: use of monoclonal antibodies to identify and isolate an epimastigote specific glycoprotein. Mol. Biochem. Parasitol 3, 343–356
    OpenUrlCrossRefPubMedWeb of Science
    1. Vickerman K.,
    2. Tetley L.,
    3. Hendry K. A. K. and
    4. Turner C. M. R.
    (1988). Biology of African trypanosomes in the tsetse fly. Biol. Cell 64, 109–119
    OpenUrlCrossRefPubMedWeb of Science
    1. Warburg A.,
    2. Tesh R. B. and
    3. McMahon-Pratt D.
    (1989). Studies on theattachment of Leishmania flagella to sand-fly midgut epithelium. J. Protozool 36, 613–617
    OpenUrlCrossRefPubMedWeb of Science
Back to top

 Download PDF

Email
Journal Articles
Gene deletion suggests a role for Trypanosoma cruzi surface glycoprotein GP72 in the insect and mammalian stages of the life cycle
A.R. de Jesus, R. Cooper, M. Espinosa, J.E. Gomes, E.S. Garcia, S. Paul, G.A. Cross
Journal of Cell Science 1993 106: 1023-1033;
del.icio.us logo Digg logo Reddit logo Twitter logo CiteULike logo Facebook logo Google logo Mendeley logo
Citation Tools
Alerts

Article navigation

Other journals from The Company of Biologists

Advertisement

First Person interviews

Photo collage of Chen Yu, Sushmita Chatterjee, Ruiqi Wang and Lotte Vanheer.

Have you seen our First Person interviews with the early-career first authors of our papers? The authors talk about their work in and out of the lab, the journeys that led them to where they are now and the scientists who inspired them along the way. Recently, we caught up with first authors Maitreyi Rathod, Sushmita Chatterjee, Lotte Vanheer, Rachel Furlong, Pamela Adami, Ruiqi Wang and Chen Yu.

Travelling Fellowship – New imaging approach unveils a bigger picture

Highlights from Travelling Fellowship trips

Find out how Pamela Imperadore’s Travelling Fellowship grant from The Company of Biologists took her to Germany, where she used new imaging techniques to investigate the cellular machinery underlying octopus arm regeneration. Don’t miss the next application deadline for 2020 travel, coming up on 29 November. Where will your research take you?

preLights – Meet the preLighters: an interview with Maiko Kitaoka

Maiko Kitaoka

Maiko Kitaoka is a graduate student in the lab of Rebecca Heald at the University of California, Berkeley. Here she studies the cause of chromosome mis-segregation defects in Xenopus hybrids. We caught up with Maiko to discuss her research, science communication, ballet, preprints and more.

Journal Meeting – Cell Dynamics: Host-Pathogen Interface

Registration is now open for the third instalment of the highly successful Cellular Dynamics Meeting Series, and will focus on ‘Host-Pathogen Interface’. The meeting will take place 17-20 May 2020, and further information is available here.

Cell Science at a Glance – Adaptor protein complexes and disease at a glance

A new poster from the Robinson lab summarises what is known about the five adaptor protein complexes and discuss how this helps to explain the clinical features of different genetic disorders.

JCS joins the Review Commons initiative

Journal of Cell Science is pleased to be a part of the new and exciting Review Commons initiative, launched by EMBO and ASAPbio. Streamlining the publishing process, Review Commons enables high-quality peer review to take place before journal submission. Papers submitted to Review Commons will be assessed independently of any journal, focusing solely on the paper’s scientific rigor and merit.