Autor(es): Galinski, Mary R ; Ingravallo, Paul ; Corredor-Medina, Claudia ; Al-Khedery, Basima ; P?voa, Marinete Marins ; Barnwell, John W
Data: 2021
Origem: Oasisbr
Assunto(s): Plasmodium vivax / parasitologia; Prote?na 1 de Superf?cie de Merozoito; Sequ?ncia de Amino?cidos
The National Institutes of Allergy and Infectious Diseases of the National Institutes of Health (AI24710-14), the UNDP/WORLD BANK/WHO Special Programme for Research and in Tropical Diseases (TDR), and the US Agency for International Development Malaria Vaccine Development Program
Emory University. Department of Medicine. Emory Vaccine Research Center. Yerkes Primate Research Center. Atlanta, GA, USA.
New York University. School of Medicine. New York, NY, USA.
Emory University. Department of Medicine. Emory Vaccine Research Center. Yerkes Primate Research Center. Atlanta, GA, USA.
Emory University. Department of Medicine. Emory Vaccine Research Center. Yerkes Primate Research Center. Atlanta, GA, USA.
Minist?rio da Sa?de. Funda??o Nacional de Sa?de. Instituto Evandro Chagas. Bel?m, PA, Brasil.
Centers for Disease Control and Prevention. Division of Parasitic Diseases. Chamblee, GA, USA.
The genes encoding two merozoite surface proteins of Plasmodium i ax that are related to PvMSP3 [1] are reported. One of these genes was identified within P. i ax gt11 clone 5.4, which was selected by immunoscreening with a Saimiri monkey antiserum. The insert DNA of this clone was used as a probe to isolate the complete gene from a P. i ax DASH genomic (g) DNA library. Antibodies to recombinant 5.4 and subsequent fusion proteins produce a pattern of circumferential surface fluorescence by indirect immunofluorescence assays (IFA) on segmented schizonts and free intact merozoites, and recognize a 125 kDa protein via western immunoblots. The gene, however, encodes a protein with a calculated size of 75 677 Da, and 3 and 5 RACE analyses were employed to confirm the size of the gene and its coding region. The second related P. i ax gene was isolated by hybridization of a fragment of an orthologous P. knowlesi gene. The encoded proteins of all three related P. i ax genes have putative signal peptides, large central domains that contain 20% alanine residues bound by charged regions, are predicted to form -helices with heptad repeat coiled-coil structures, and do not have a hydrophobic region that could anchor them to the surface of the merozoite. Although the overall identity in amino acid alignment among the three encoded proteins is low (40%), the shared predicted structural features and motifs indicate that they are members of an intra-species family, which we are designating as the PvMSP-3 family with the reported members being Pvmsp-3, Pvmsp-3 , and Pvmsp-3. We further demonstrate that this family also includes related proteins from P. knowlesi and P. falciparum
