scholarly journals Identification of B Cell Epitopes of a 30kDa Babesia equi Merozoite Surface Protein.

1998 ◽  
Vol 60 (5) ◽  
pp. 563-567 ◽  
Author(s):  
Yasuko HANAFUSA ◽  
Tomoko SUDO ◽  
Yasuhito SAKO ◽  
Takumi KANEMARU ◽  
Masanobu KAMADA ◽  
...  
Keyword(s):  
B Cell ◽  
Surface Protein ◽  
Merozoite Surface Protein ◽  
B Cell Epitopes ◽  
Babesia Equi

scholarly journals Characterization of Conserved T- and B-Cell Epitopes in Plasmodium falciparum Major Merozoite Surface Protein 1

2000 ◽  
Vol 68 (5) ◽  
pp. 2685-2691 ◽  
Author(s):  
Marcela Parra ◽  
George Hui ◽  
Armead H. Johnson ◽  
Jay A. Berzofsky ◽  
Theodore Roberts ◽  
...  
Keyword(s):  
T Cells ◽  
T Cell ◽  
B Cell ◽  
Surface Protein ◽  
T Cell Responses ◽  
Merozoite Surface Protein ◽  
B Cell Epitopes ◽  
Conserved Sequence ◽  
Cell Responses ◽  
Merozoite Surface Protein 1

ABSTRACT Vaccines for P. falciparum will need to contain both T- and B-cell epitopes. Conserved epitopes are the most desirable, but they are often poorly immunogenic. The major merozoite surface protein 1 (MSP-1) is currently a leading vaccine candidate antigen. In this study, six peptides from conserved or partly conserved regions of MSP-1 were evaluated for immunogenicity in B10 congenic mice. Following immunization with the peptides, murine T cells were tested for the ability to proliferate in vitro and antibody responses to MSP-1 were evaluated in vivo. The results showed that one highly conserved sequence (MSP-1#1, VTHESYQELVKKLEALEDAV; located at amino acid positions 20 to 39) and one partly conserved sequence (MSP-1#23, GLFHKEKMILNEEEITTKGA; located at positions 44 to 63) contained both T- and B-cell epitopes. Immunization of mice with these peptides resulted in T-cell proliferation and enhanced production of antibody to MSP-1 upon exposure to merozoites. MSP-1#1 stimulated T-cell responses in three of the six strains of mice evaluated, whereas MSP-1#23 was immunogenic in only one strain. Immunization with the other four peptides resulted in T-cell responses to the peptides, but none of the resulting peptide-specific T cells recognized native MSP-1. These results demonstrate that two sequences located in the N terminus of MSP-1 can induce T- and B-cell responses following immunization in a murine model. Clearly, these sequences merit further consideration for inclusion in a vaccine for malaria.

scholarly journals In Vivo Expression and Immunological Studies of the 42-Kilodalton Carboxyl-Terminal Processing Fragment of Plasmodium falciparum Merozoite Surface Protein 1 in the Baculovirus-Silkworm System

2002 ◽  
Vol 70 (6) ◽  
pp. 2772-2779 ◽  
Author(s):  
Alan L. Y. Pang ◽  
Caryn N. Hashimoto ◽  
Leslie Q. Tam ◽  
Z. Q. Meng ◽  
George S. N. Hui ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
B Cell ◽  
Expression System ◽  
Surface Protein ◽  
Merozoite Surface Protein ◽  
Enzyme Linked Immunosorbent Assay ◽  
Attractive Alternative ◽  
B Cell Epitopes ◽  
Merozoite Surface Protein 1 ◽  
Carboxyl Terminal

ABSTRACT The 42-kDa carboxyl-terminal processing fragment of Plasmodium falciparum merozoite surface protein 1 (MSP-142) is an anti-erythrocytic stage malaria vaccine candidate. In this study, MSP-142 was expressed by using the Bombyx mori nuclear polyhedrosis virus-silkworm expression system, and the antigenicity and immmunogenicity of the recombinant protein, Bmp42, were evaluated. The average yield of Bmp42, as determined by a sandwich enzyme-linked immunosorbent assay (ELISA), was 379 μg/ml of infected silkworm hemolymph, which was >100-fold higher than the level attainable in cell culture medium. N-terminal amino acid sequencing revealed that Bmp42 was correctly processed in silkworm cells. Data from immunoblotting, as well as from the inhibition ELISA, suggested that the conformational B-cell epitopes of MSP-142 were recreated in Bmp42. Immunization of rabbits with Bmp42 in complete Freund's adjuvant generated high-titer antibody responses against the immunogen. Specificity analyses of the anti-Bmp42 antibodies using several recombinant MSP-119 proteins expressing variant and conserved B-cell epitopes suggested that the anti-Bmp42 antibodies recognized primarily conserved epitopes on MSP-119. Furthermore, the anti-Bmp42 antibodies were highly effective in inhibiting the in vitro growth of parasites carrying homologous or heterologous MSP-142. Our results demonstrated that the baculovirus-silkworm expression system could be employed to express biologically and immunologically active recombinant MSP-142 at elevated levels; thus, it is an attractive alternative for producing a protective MSP-142 vaccine for human use.

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 The acquisition of long-lived memory B cell responses to merozoite surface protein-8 in individuals with Plasmodium vivax infection

2019 ◽  
Vol 18 (1) ◽  
Author(s):  
Piyawan Kochayoo ◽  
Natthapon Kittisenachai ◽  
Siriruk Changrob ◽  
Kittikorn Wangriatisak ◽  
Fauzi Muh ◽  
...  
Keyword(s):  
B Cell ◽  
Plasmodium Vivax ◽  
Surface Protein ◽  
Merozoite Surface Protein ◽  
Vivax Infection ◽  
Memory B Cell ◽  
Cell Responses ◽  
B Cell Responses

scholarly journals Identification of B-cell epitopes of Borrelia burgdorferi outer surface protein C by screening a phage-displayed gene fragment library

2016 ◽  
Vol 60 (10) ◽  
pp. 669-677 ◽  
Author(s):  
Lucia Pulzova ◽  
Zuzana Flachbartova ◽  
Elena Bencurova ◽  
Lenka Potocnakova ◽  
Lubos Comor ◽  
...  
Keyword(s):  
Borrelia Burgdorferi ◽  
B Cell ◽  
Outer Surface ◽  
Protein C ◽  
Surface Protein ◽  
Gene Fragment ◽  
B Cell Epitopes ◽  
Outer Surface Protein ◽  
Fragment Library

scholarly journals Prediction and Evolution of B Cell Epitopes of Surface Protein in SARS-CoV-2

2020 ◽  
Author(s):  
Jerome R Lon ◽  
Yunmeng Bai ◽  
Bingxu Zhong ◽  
Fuqaing Cai ◽  
Hongli Du
Keyword(s):  
B Cell ◽  
Vaccine Development ◽  
Surface Protein ◽  
The Other ◽  
Reference Sequence ◽  
Prediction Methods ◽  
Whole Genome ◽  
B Cell Epitopes ◽  
Conformational Epitopes ◽  
Linear Epitopes

AbstractThe discovery of epitopes is helpful to the development of SARS-CoV-2 vaccine. The sequences of the surface protein of SARS-CoV-2 and its proximal sequences were obtained by BLAST, the sequences of the whole genome of SARS-CoV-2 were obtained from the GenBank. Based on the NCBI Reference Sequence: NC_045512.2, the conformational and linear B cell epitopes of the surface protein were predicted separately by various prediction methods. Furthermore, the conservation of the epitopes, the adaptability and other evolutionary characteristics were also analyzed. 7 epitopes were predicted, including 5 linear epitopes and 2 conformational epitopes, one of the linear and one of the conformational were coincide. The epitope D mutated easily, but the other epitopes were very conservative and the epitope C was the most conservative. It is worth mentioning that all of the 6 dominated epitopes were absolutely conservative in nearly 1000 SARS-CoV-2 genomes, and they deserved further study. The findings would facilitate the vaccine development, had the potential to be directly applied on the treatment in this disease, but also have the potential to prevent the possible threats caused by other types of coronavirus.

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