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Science 14 March 1986:
Vol. 231. no. 4743, pp. 1299 - 1302
DOI: 10.1126/science.3945825
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Articles

Science, Vol 231, Issue 4743, 1299-1302
Copyright © 1986 by American Association for the Advancement of Science

articles

Immunization with an isolate-common surface protein protects cattle against anaplasmosis

GH Palmer, AF Barbet, WC Davis, and TC McGuire

Hemoparasitic diseases are endemic in half the world's livestock production areas and are the greatest obstacle to improved meat, milk, and fiber production in the Third World. The most prevalent of these diseases, anaplasmosis, occurs throughout tropical and subtropical regions and is responsible for 50,000 to 100,000 cattle deaths annually in the United States alone. Despite its prevalence and the severity of the losses, an effective immunoprophylaxis for anaplasmosis has not been developed. A neutralization-sensitive epitope on a surface protein with a molecular weight of 105,000 (Am 105) of the causative rickettsia Anaplasma marginale was identified by monoclonal antibody inhibition of infectivity. This epitope was determined to be common to eight isolates with antigenic, morphologic, and protein structural differences. Cattle immunized with Am 105 purified by immunoaffinity chromatography were protected against challenge with virulent Anaplasma marginale. The identification of Am 105 as bearing isolate-common epitopes capable of inducing protection in immunized cattle provides the basis for the development of an effective subunit vaccine for bovine anaplasmosis.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Composition of the Surface Proteome of Anaplasma marginale and Its Role in Protective Immunity Induced by Outer Membrane Immunization.
S. M. Noh, K. A. Brayton, W. C. Brown, J. Norimine, G. R. Munske, C. M. Davitt, and G. H. Palmer (2008)
Infect. Immun. 76, 2219-2226
   Abstract »    Full Text »    PDF »
Physical Linkage of Naturally Complexed Bacterial Outer Membrane Proteins Enhances Immunogenicity.
H. Macmillan, J. Norimine, K. A. Brayton, G. H. Palmer, and W. C. Brown (2008)
Infect. Immun. 76, 1223-1229
   Abstract »    Full Text »    PDF »
Identification of Novel Surface Proteins of Anaplasma phagocytophilum by Affinity Purification and Proteomics.
Y. Ge and Y. Rikihisa (2007)
J. Bacteriol. 189, 7819-7828
   Abstract »    Full Text »    PDF »
Surface-Exposed Proteins of Ehrlichia chaffeensis.
Y. Ge and Y. Rikihisa (2007)
Infect. Immun. 75, 3833-3841
   Abstract »    Full Text »    PDF »
Immunogenicity of Anaplasma marginale Type IV Secretion System Proteins in a Protective Outer Membrane Vaccine.
J. E. Lopez, G. H. Palmer, K. A. Brayton, M. J. Dark, S. E. Leach, and W. C. Brown (2007)
Infect. Immun. 75, 2333-2342
   Abstract »    Full Text »    PDF »
Analysis of the Anaplasma marginale Major Surface Protein 1 Complex Protein Composition by Tandem Mass Spectrometry.
H. Macmillan, K. A. Brayton, G. H. Palmer, T. C. McGuire, G. Munske, W. F. Siems, and W. C. Brown (2006)
J. Bacteriol. 188, 4983-4991
   Abstract »    Full Text »    PDF »
Two Monoclonal Antibodies with Defined Epitopes of P44 Major Surface Proteins Neutralize Anaplasma phagocytophilum by Distinct Mechanisms.
X. Wang, T. Kikuchi, and Y. Rikihisa (2006)
Infect. Immun. 74, 1873-1882
   Abstract »    Full Text »    PDF »
Identification of Novel Antigenic Proteins in a Complex Anaplasma marginale Outer Membrane Immunogen by Mass Spectrometry and Genomic Mapping.
J. E. Lopez, W. F. Siems, G. H. Palmer, K. A. Brayton, T. C. McGuire, J. Norimine, and W. C. Brown (2005)
Infect. Immun. 73, 8109-8118
   Abstract »    Full Text »    PDF »
Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins.
K. A. Brayton, L. S. Kappmeyer, D. R. Herndon, M. J. Dark, D. L. Tibbals, G. H. Palmer, T. C. McGuire, and D. P. Knowles Jr. (2005)
PNAS 102, 844-849
   Abstract »    Full Text »    PDF »
Antigens and Alternatives for Control of Anaplasma marginale Infection in Cattle.
K. M. Kocan, J. de la Fuente, A. A. Guglielmone, and R. D. Melendez (2003)
Clin. Microbiol. Rev. 16, 698-712
   Abstract »    Full Text »    PDF »
Kinetics of Antibody Response to Ehrlichia canis Immunoreactive Proteins.
J. W. McBride, R. E. Corstvet, S. D. Gaunt, C. Boudreaux, T. Guedry, and D. H. Walker (2003)
Infect. Immun. 71, 2516-2524
   Abstract »    Full Text »    PDF »
Major Histocompatibility Complex Class II DR-Restricted Memory CD4+ T Lymphocytes Recognize Conserved Immunodominant Epitopes of Anaplasma marginale Major Surface Protein 1a.
W. C. Brown, T. C. McGuire, W. Mwangi, K. A. Kegerreis, H. Macmillan, H. A. Lewin, and G. H. Palmer (2002)
Infect. Immun. 70, 5521-5532
   Abstract »    Full Text »    PDF »
DNA-Encoded Fetal Liver Tyrosine Kinase 3 Ligand and Granulocyte Macrophage-Colony-Stimulating Factor Increase Dendritic Cell Recruitment to the Inoculation Site and Enhance Antigen-Specific CD4+ T Cell Responses Induced by DNA Vaccination of Outbred Animals.
W. Mwangi, W. C. Brown, H. A. Lewin, C. J. Howard, J. C. Hope, T. V. Baszler, P. Caplazi, J. Abbott, and G. H. Palmer (2002)
J. Immunol. 169, 3837-3846
   Abstract »    Full Text »    PDF »
CD4+ T Lymphocytes from Calves Immunized with Anaplasma marginale Major Surface Protein 1 (MSP1), a Heteromeric Complex of MSP1a and MSP1b, Preferentially Recognize the MSP1a Carboxyl Terminus That Is Conserved among Strains.
W. C. Brown, G. H. Palmer, H. A. Lewin, and T. C. McGuire (2001)
Infect. Immun. 69, 6853-6862
   Abstract »    Full Text »    PDF »
Analysis of the 16S rRNA Gene Sequence of Anaplasma centrale and Its Phylogenetic Relatedness to Other Ehrlichiae.
H. Inokuma, Y. Terada, T. Kamio, D. Raoult, and P. Brouqui (2001)
Clin. Vaccine Immunol. 8, 241-244
   Abstract »    Full Text »    PDF »
Expression of Polymorphic msp1beta Genes during Acute Anaplasma marginale Rickettsemia.
M. Camacho-Nuez, M. de Lourdes Munoz, C. E. Suarez, T. C. McGuire, W. C. Brown, and G. H. Palmer (2000)
Infect. Immun. 68, 1946-1952
   Abstract »    Full Text »    PDF »
Biased Immunoglobulin G1 Isotype Responses Induced in Cattle with DNA Expressing msp1a of Anaplasma marginale.
A. Arulkanthan, W. C. Brown, T. C. McGuire, and D. P. Knowles (1999)
Infect. Immun. 67, 3481-3487
   Abstract »    Full Text »    PDF »
Comparison of Surface Proteins of Anaplasma marginale Grown in Tick Cell Culture, Tick Salivary Glands, and Cattle.
A. F. Barbet, R. Blentlinger, J. Yi, A. M. Lundgren, E. F. Blouin, and K. M. Kocan (1999)
Infect. Immun. 67, 102-107
   Abstract »    Full Text »    PDF »
CD4+ T-Lymphocyte and Immunoglobulin G2 Responses in Calves Immunized with Anaplasma marginale Outer Membranes and Protected against Homologous Challenge.
W. C. Brown, V. Shkap, D. Zhu, T. C. McGuire, W. Tuo, T. F. McElwain, and G. H. Palmer (1998)
Infect. Immun. 66, 5406-5413
   Abstract »    Full Text »    PDF »
The Repertoire of Anaplasma marginale Antigens Recognized by CD4+ T-Lymphocyte Clones from Protectively Immunized Cattle Is Diverse and Includes Major Surface Protein 2 (MSP-2) and MSP-3.
W. C. Brown, D. Zhu, V. Shkap, T. C. McGuire, E. F. Blouin, K. M. Kocan, and G. H. Palmer (1998)
Infect. Immun. 66, 5414-5422
   Abstract »    Full Text »    PDF »
Conformational Dependence of Anaplasma marginale Major Surface Protein 5 Surface-Exposed B-Cell Epitopes.
D. Munodzana, T. F. McElwain, D. P. Knowles, and G. H. Palmer (1998)
Infect. Immun. 66, 2619-2624
   Abstract »    Full Text »    PDF »
Expression of Anaplasma marginale Major Surface Protein 2 Variants during Persistent Cyclic Rickettsemia.
D. M. French, T. F. McElwain, T. C. McGuire, and G. H. Palmer (1998)
Infect. Immun. 66, 1200-1207
   Abstract »    Full Text »    PDF »


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