Hostname: page-component-76fb5796d-qxdb6 Total loading time: 0 Render date: 2024-04-26T17:15:21.030Z Has data issue: false hasContentIssue false

Antigen shedding from the surface of the infective stage larvae of Dirofilaria immitis

Published online by Cambridge University Press:  06 April 2009

M. S. Ibrahim
Affiliation:
Department of Immunology and Infectious Diseases, The Johns Hopkins University School of Hygiene and Public Health, 615 North Wolfe Street, Baltimore, MD 21205
W. K. Tamashiro
Affiliation:
Department of Immunology and Infectious Diseases, The Johns Hopkins University School of Hygiene and Public Health, 615 North Wolfe Street, Baltimore, MD 21205
D. A. Moraga
Affiliation:
Department of Immunology and Infectious Diseases, The Johns Hopkins University School of Hygiene and Public Health, 615 North Wolfe Street, Baltimore, MD 21205
A. L. Scott
Affiliation:
Department of Immunology and Infectious Diseases, The Johns Hopkins University School of Hygiene and Public Health, 615 North Wolfe Street, Baltimore, MD 21205

Summary

A qualitative and quantitative analysis was made of the release of surface-associated molecules from developing Dirofilaria immitis infective-stage larvae (L3). D. immitis L3s were labelled with 125I using an Iodogen catalysed reaction and either maintained in culture or placed in chambers that were implanted into Lewis rats. The larvae released 10–20% of the labelled material each day during the first 4 days of in vitro and in vivo development. The loss of surface-labelled peptides from developing larvae corresponded with an increase in the amount of trichloroacetic acid-precipitable radioactivity found in the culture medium. SDS—PAGE analysis of the labelled material showed that the same 35 and 6 kDa components found in larval extracts were shed into culture medium by the developing parasites. Metabolic labelling studies and experiments in which larvae were labelled after different times in culture indicated that, once released, the surfaceassociated molecules were not replaced, and that this net loss of surface peptides resulted in a reduction in the antigenic potential of the cuticular surface. Antibodies from both immunized rabbits and naturally infected dogs immunoprecipitated the 35 kDa component. In contrast, the 6 kDa molecule was not recognized by the antibodies in any of the sera tested. Shedding of surface peptides and reducing surface antigenicity may represent mechanisms by which D. immitis infective-stage larvae evade immune attack.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1989

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Abraham, D., Grieve, R. B., & Mika-Grieve, M., (1988). Dirofilaria immitis: surface properties of third- and fourth-stage larvae. Experimental Parasitology 65, 157–67.CrossRefGoogle ScholarPubMed
Betschart, B., & Jenkins, J. M., (1987). Distribution of iodinated proteins in Dipetalonema viteae after surface labelling. Molecular and Biochemical Parasitology 22, 18.Google Scholar
Carlow, C. K. S., Perrone, J., Spielman, A., & Philipp, M., (1987). A developmentally regulated surface epitope expressed by the infective larva of Brugia malayi which is rapidly lost after infection. UCLA Symposium on Molecular and Cellular Biology 60, 301–10.Google Scholar
Devaney, E., (1985). Dirofilaria immitis: the molting of the infective larvae in vitro. Journal of Helminthology 59, 4750.Google Scholar
Devaney, E., (1988). Biochemical and immunochemical characterization of the 30 kilodalton surface antigen of Brugia pahangi. Molecular and Biochemical Parasitology 27, 8392.Google Scholar
Ibrahim, M. S., & Trpis, M., (1987). The effect of Brugia pahangi infection on survival of susceptible and refractory species of the Aedes scutellaris complex. Medical and Veterinary Entomology 1, 329–37.Google Scholar
Kaushal, N. A., Hussain, R., Nash, T. E., & Ottesen, E. A., (1982). Identification and characterization of excretory—secretory products of Brugia malayi adult filarial parasites. Journal of Immunology 29, 338–43.Google Scholar
Laemmli, U. K., (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, London 227, 680–5.CrossRefGoogle ScholarPubMed
Maizels, R. M., Desavigny, D., & Ogilvie, B. M., (1984). Characterization of surface and excretory—secretory antigens of Toxocara canis infective larvae. Parasite Immunology 6, 2337.Google Scholar
Maizels, R., Burke, J., Sutano, I., Purnomo, , & Partono, F., (1986). Secreted and surface antigens from larval stages of Wuchereria bancrofti, the major human lymphatic filariasis. Molecular and Biochemical Parasitology 19, 2734.CrossRefGoogle Scholar
Marshall, E., & Howells, R. E., (1986). Turnover of the surface proteins of adult and third and fourth stage larval Brugia pahangi. Molecular and Biochemical Parasitology 18, 1724.Google Scholar
Pearce, E. J., Basch, P. F., & Sher, A., (1986). Evidence that the reduced surface antigenicity of developing Schistosoma mansoni schistosomula is due to antigen shedding rather than acquisition of host molecules. Parasite Immunology 8, 7994.CrossRefGoogle Scholar
Philipp, M., & Davis, T. B., (1986). Biochemical and immunologic characterization of a major surface antigen of Dirofilaria immitis infective larvae. Journal of Immunology 136, 2621–7.Google Scholar
Philipp, M., Parkhouse, R. M. E., & Ogilvie, B. M., (1980). Changing proteins on the surface of a parasite nematode. Nature, London 287, 538–40.CrossRefGoogle Scholar
Philipp, M., & Rumjaneck, F. D., (1984). Antigenic and dynamic properties of helminth surface structures. Molecular and Biochemical Parasitology 10, 254–68.Google Scholar
Staniunas, R. J., & Hammerberg, B., (1982). Diethylcarbamazine-enhanced activation of complement by intact microfilariae of Dirofilaria immitis and their in vitro products. Journal of Parasitology 68, 809–16.Google Scholar