scholarly journals Major-surface-protein-4-gene-based detection of Anaplasma marginale isolated from sheep in Al-Diwaniyah province, Iraq

2021 ◽  
Vol 36 (1) ◽  
pp. 85-88
Author(s):  
Saba F. Klaif ◽  
Asaad J. Abid ◽  
Monyer A. Al-Fatlawi ◽  
Mansoor J. Ali
Keyword(s):  
Surface Protein ◽  
Anaplasma Marginale ◽  
Major Surface Protein ◽  
Major Surface

scholarly journals Anaplasma marginale Major Surface Protein 2 CD4+-T-Cell Epitopes Are Evenly Distributed in Conserved and Hypervariable Regions (HVR), Whereas Linear B-Cell Epitopes Are Predominantly Located in the HVR

2004 ◽  
Vol 72 (12) ◽  
pp. 7360-7366 ◽  
Author(s):  
Jeffrey R. Abbott ◽  
Guy H. Palmer ◽  
Chris J. Howard ◽  
Jayne C. Hope ◽  
Wendy C. Brown
Keyword(s):  
T Cell ◽  
B Cell ◽  
Surface Protein ◽  
Anaplasma Marginale ◽  
T Cell Epitopes ◽  
B Cell Epitopes ◽  
Major Surface Protein ◽  
Hypervariable Regions ◽  
Major Surface ◽  
Linear B

ABSTRACT Organisms in the genus Anaplasma express an immunodominant major surface protein 2 (MSP2), composed of a central hypervariable region (HVR) flanked by highly conserved regions. Throughout Anaplasma marginale infection, recombination results in the sequential appearance of novel MSP2 variants and subsequent control of rickettsemia by the immune response, leading to persistent infection. To determine whether immune evasion and selection for variant organisms is associated with a predominant response against HVR epitopes, T-cell and linear B-cell epitopes were localized by measuring peripheral blood gamma interferon-secreting cells, proliferation, and antibody binding to 27 overlapping peptides spanning MSP2 in 16 cattle. Similar numbers of MSP2-specific CD4+ T-cell epitopes eliciting responses of similar magnitude were found in conserved and hypervariable regions. T-cell epitope clusters recognized by the majority of animals were identified in the HVR (amino acids [aa] 171 to 229) and conserved regions (aa 101 to 170 and 272 to 361). In contrast, linear B-cell epitopes were concentrated in the HVR, residing within hydrophilic sequences. The pattern of recognition of epitope clusters by T cells and of HVR epitopes by B cells is consistent with the influence of protein structure on epitope recognition.

scholarly journals Comparison between indirect enzyme-linked immunosorbent assays for Anaplasma marginale antibodies with recombinant major surface protein 5 and initial body antigens

2006 ◽  
Vol 101 (5) ◽  
pp. 511-516 ◽  
Author(s):  
Virgínia MG Silva ◽  
Flábio R Araújo ◽  
Claudio R Madruga ◽  
Cleber O Soares ◽  
Raul H Kessler ◽  
...  
Keyword(s):  
Surface Protein ◽  
Anaplasma Marginale ◽  
Major Surface Protein ◽  
Immunosorbent Assays ◽  
Major Surface

Phylogeography of New World isolates of Anaplasma marginale based on major surface protein sequences

2002 ◽  
Vol 88 (3) ◽  
pp. 275-285 ◽  
Author(s):  
José de la Fuente ◽  
Ronald A Van Den Bussche ◽  
Jose C Garcia-Garcia ◽  
Sergio D Rodrı́guez ◽  
Miguel A Garcı́a ◽  
...  
Keyword(s):  
New World ◽  
Protein Sequences ◽  
Surface Protein ◽  
Anaplasma Marginale ◽  
Major Surface Protein ◽  
Major Surface

scholarly journals Interleukin-12 as an Adjuvant Promotes Immunoglobulin G and Type 1 Cytokine Recall Responses to Major Surface Protein 2 of the Ehrlichial Pathogen Anaplasma marginale

2000 ◽  
Vol 68 (1) ◽  
pp. 270-280 ◽  
Author(s):  
Wenbin Tuo ◽  
Guy H. Palmer ◽  
Travis C. McGuire ◽  
Daming Zhu ◽  
Wendy C. Brown
Keyword(s):  
Protective Immunity ◽  
Mononuclear Cells ◽  
Surface Protein ◽  
Anaplasma Marginale ◽  
Interleukin 12 ◽  
Major Surface Protein ◽  
Ifn Γ ◽  
Major Surface ◽  
Type 1 Cytokine

ABSTRACT Anaplasma marginale is a tick-transmitted pathogen of cattle closely related to the human ehrlichiae, Ehrlichia chaffeensis and the agent of human granulocytic ehrlichiosis (HGE). These pathogens have in common a structurally conserved outer membrane protein (OMP) designated the major surface protein 2 (MSP-2) in A. marginale and HGE and OMP-1 in E. chaffeensis. Protective immunity against ehrlichial pathogens is believed to require induction of gamma interferon (IFN-γ) and opsonizing immunoglobulin (Ig) subclasses directed against OMP epitopes that, in concert, activate macrophages for phagocytosis and killing. Because interleukin-12 (IL-12) acts as an adjuvant for protein immunization to induce IFN-γ and protective immunity against intracellular pathogens, we hypothesized that as an adjuvant with MSP-2, IL-12 would augment type 1 recall responses to A. marginale. IL-12 was coadsorbed with MSP-2 to alum and shown to significantly enhance IFN-γ production by lymph node cells (LNC) and LNC-derived CD4+ T-cell lines from immunized calves following recall stimulation with A. marginale. LNC proliferation and IL-2 production were also enhanced in IL-12-treated calves. Elevated recall proliferative responses by peripheral blood mononuclear cells were still evident 9 months after immunization. Serum IgG levels were consistently increased in IL-12 immunized calves, predominantly due to higher IgG1 responses. The results support the use of IL-12 coadsorbed with OMP of ehrlichial pathogens in alum to amplify both antibody and type-1 cytokine responses important for protective immunity.

scholarly journals Characterization of Anaplasma phagocytophilum Major Surface Protein 5 and the Extent of Its Cross-Reactivity with A. marginale

2007 ◽  
Vol 14 (3) ◽  
pp. 262-268 ◽  
Author(s):  
N. I. Strik ◽  
A. R. Alleman ◽  
A. F. Barbet ◽  
H. L. Sorenson ◽  
H. L. Wamsley ◽  
...  
Keyword(s):  
United States ◽  
Anaplasma Phagocytophilum ◽  
Indirect Elisa ◽  
Surface Protein ◽  
Anaplasma Marginale ◽  
The United States ◽  
Cross Reactivity ◽  
Serum Samples ◽  
Major Surface Protein ◽  
Major Surface

ABSTRACT Major surface protein 5 (Msp5) of Anaplasma marginale is highly conserved in the genus Anaplasma and the antigen used in a commercially available competitive enzyme-linked immunosorbent assay (cELISA) for serologic identification of cattle with anaplasmosis. This study analyzes the degrees of conservation of Msp5 among various isolates of Anaplasma phagocytophilum and the extent of serologic cross-reactivity between recombinant Msp5 (rMsp5) of Anaplasma marginale and A. phagocytophilum. The msp5 genes from various isolates of A. phagocytophilum were sequenced and compared. rMsp5 proteins of A. phagocytophilum and A. marginale were used separately in an indirect ELISA to detect cross-reactivity in serum samples from humans and dogs infected with A. phagocytophilum and cattle infected with A. marginale. Serum samples were also tested with a commercially available competitive ELISA that uses monoclonal antibody ANAF16C1. There were 100% sequence identities in the msp5 genes among all of the A. phagocytophilum isolates from the United States and a horse isolate from Sweden. Sheep isolates from Norway and dog isolates from Sweden were 99% identical to one another but differed in 17 base pairs from the United States isolates and the horse isolate. Serologic cross-reactivity was identified when serum samples from cattle infected with A. marginale were reacted with rMsp5 of A. phagocytophilum and when serum samples from humans and dogs infected with A. phagocytophilum were reacted with rMsp5 of A. marginale in an indirect-ELISA format. Serum samples from dogs or humans infected with A. phagocytophilum did not cross-react with rMsp5 of A. marginale when tested with the commercially available cELISA. These results suggest that rMsp5 of A. phagocytophilum is highly conserved among United States and European isolates and that serologic distinction between A. phagocytophilum and A. marginale infections cannot be accomplished if rMsp5 from either organism is used in an indirect ELISA.

Analysis of world strains of Anaplasma marginale using major surface protein 1a repeat sequences

2007 ◽  
Vol 119 (2-4) ◽  
pp. 382-390 ◽  
Author(s):  
José de la Fuente ◽  
Paula Ruybal ◽  
Moses S. Mtshali ◽  
Victoria Naranjo ◽  
Li Shuqing ◽  
...  
Keyword(s):  
Surface Protein ◽  
Anaplasma Marginale ◽  
Major Surface Protein ◽  
Repeat Sequences ◽  
Major Surface

scholarly journals Characterization of Anaplasma marginale Isolated from North American Bison

2003 ◽  
Vol 69 (8) ◽  
pp. 5001-5005 ◽  
Author(s):  
José de la Fuente ◽  
Elizabeth J. Golsteyn Thomas ◽  
Ronald A. Van Den Bussche ◽  
Robert G. Hamilton ◽  
Elaine E. Tanaka ◽  
...  
Keyword(s):  
New World ◽  
Surface Protein ◽  
Anaplasma Marginale ◽  
The United States ◽  
Bison Bison ◽  
Infected Cattle ◽  
Major Surface Protein ◽  
The World ◽  
Major Surface

ABSTRACT Anaplasma marginale (Rickettsiales: Anaplasmataceae), a tick-borne pathogen of cattle, is endemic in tropical and subtropical regions of the world. Although serologic tests have identified American bison, Bison bison, as being infected with A. marginale, the present study was undertaken to confirm A. marginale infection and to characterize isolates obtained from naturally infected bison in the United States and Canada. Major surface protein (MSP1a and MSP4) sequences of bison isolates were characterized in comparison with New World cattle isolates. Blood from one U.S. bison was inoculated into a susceptible, splenectomized calf, which developed acute anaplasmosis, demonstrating infectivity of this A. marginale bison isolate for cattle. The results of this study showed that these A. marginale isolates obtained from bison were similar to ones from naturally infected cattle.

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

1996 ◽  
Vol 64 (3) ◽  
pp. 836-841 ◽  
Author(s):  
G Eid ◽  
D M French ◽  
A M Lundgren ◽  
A F Barbet ◽  
T F McElwain ◽  
...  
Keyword(s):  
Surface Protein ◽  
Anaplasma Marginale ◽  
Major Surface Protein ◽  
Major Surface
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