» Articles » PMID: 2415457

Presence of Common Antigens, Including Major Surface Protein Epitopes, Between the Cattle (intraerythrocytic) and Tick Stages of Anaplasma Marginale

Overview
Journal Infect Immun
Date 1985 Dec 1
PMID 2415457
Citations 13
Authors
Affiliations
Soon will be listed here.
Abstract

Epitopes of major surface proteins of the intraerythrocytic cattle stage of Anaplasma marginale were demonstrated in the midgut stage of the organism within the infective tick host Dermacentor andersoni. These proteins were common to all A. marginale isolates tested and at all stages of parasitemia. Sera from cattle immunized with the tick midgut stage of A. marginale immunoprecipitated multiple-erythrocyte-stage proteins, as demonstrated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The major proteins recognized (primarily greater than 14 and less than 200 kilodaltons [kDa]) included two major-erythrocyte-stage surface proteins of 36 and 105 kDa molecular size. To confirm the presence of common tick and erythrocyte A. marginale antigens with the immunized cattle sera, we purified the 36-kDa erythrocyte-stage protein by monoclonal immunoaffinity chromatography and developed an enzyme-linked immunosorbent assay based on the purified protein. All sera from cattle immunized with tick-stage A. marginale and cattle infected with various isolates of A. marginale developed antibodies to the 36-kDa protein. The potential immunoprophylactic, diagnostic, and epidemiologic value of the major epitopes common to both the invertebrate and mammalian stages of A. marginale, especially the 36-kDa protein, is discussed.

Citing Articles

The role of nuclear technologies in the diagnosis and control of livestock diseases--a review.

Viljoen G, Luckins A Trop Anim Health Prod. 2012; 44(7):1341-66.

PMID: 22286376 PMC: 3433664. DOI: 10.1007/s11250-012-0077-5.


Composition of the surface proteome of Anaplasma marginale and its role in protective immunity induced by outer membrane immunization.

Noh S, Brayton K, Brown W, Norimine J, Munske G, Davitt C Infect Immun. 2008; 76(5):2219-26.

PMID: 18316389 PMC: 2346715. DOI: 10.1128/IAI.00008-08.


Comparison of surface proteins of Anaplasma marginale grown in tick cell culture, tick salivary glands, and cattle.

Barbet A, Blentlinger R, Yi J, Lundgren A, Blouin E, Kocan K Infect Immun. 1998; 67(1):102-7.

PMID: 9864202 PMC: 96283. DOI: 10.1128/IAI.67.1.102-107.1999.


Preliminary studies on the effect of Anaplasma marginale antibodies ingested by Dermacentor andersoni ticks (Acari:Ixodidae) with their blood meal on infections in salivary glands.

Kocan K, Blouin E, Palmer G, Eriks I, Edwards W, Claypool P Exp Appl Acarol. 1996; 20(6):297-311.

PMID: 8674360 DOI: 10.1007/BF00052960.


Expression of major surface protein 2 antigenic variants during acute Anaplasma marginale rickettsemia.

Eid G, FRENCH D, Lundgren A, Barbet A, Mcelwain T, Palmer G Infect Immun. 1996; 64(3):836-41.

PMID: 8641789 PMC: 173845. DOI: 10.1128/iai.64.3.836-841.1996.


References
1.
Bram R, Romanowski R . Recognition of Anaplasma marginale Theiler in Dermacentor andersoni Stiles (=D. venustus Marx) by the fluorescent antibody method. I. Smears of nymphal organs. J Parasitol. 1970; 56(1):32-8. View

2.
KREIER J, Ristic M . Anaplasmosis. XI. Immunoserologic characteristics of the parasites present in the blood of calves infected with the Oregon strain of Anaplasma marginale. Am J Vet Res. 1963; 24:688-96. View

3.
Shapiro S, AUGUST T . The use of immunoprecipitation to study the synthesis and cleavage processing of viral proteins. J Immunol Methods. 1976; 13(2):153-9. DOI: 10.1016/0022-1759(76)90153-8. View

4.
Peterson G . A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal Biochem. 1977; 83(2):346-56. DOI: 10.1016/0003-2697(77)90043-4. View

5.
Rovis L, Barbet A, Williams R . Characterisation of the surface coat of Trypanosoma congolense. Nature. 1978; 271(5646):654-6. DOI: 10.1038/271654a0. View