Molecular cloning and antigenic mapping of heat-shock protein 70 from the malaria species Plasmodium bergheI.
We have isolated a 70-kD heat-shock protein (hsp-70) cDNA from Plasmodium berghei. A cDNA clone encoding the P. berghei hsp-70 was isolated and sequenced, demonstrating that it is highly homologous with other Plasmodium hsp-70s. One of the common features is a series of GGMP amino acid repeats at the carboxy terminus; there is also a long, AT-rich 5' untranslated region, a hallmark of other malarial RNAs. Hydropathy and antigenicity analyses suggest the presence of two hydrophilic domains. Recombinant peptides comprising different fragments of hsp-70 were expressed in Escherichia coli and assessed for antigenicity with antiserum from mice immunized with sonicated extracts of P. berghei. Antigenic sites map to regions that include the two hydrophilic domains.
Fan
J Y
JY
Department of Biochemistry and Molecular Biology, Georgetown University Medical Center, Washington, District of Columbia, USA.
Davidson
E A
EA
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D018604:Epitope Mapping; D004926:Escherichia coli / Q000235:genetics; D005786:Gene Expression Regulation; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics* / Q000276:immunology*; D008969:Molecular Sequence Data; D010957:Plasmids; D010962:Plasmodium berghei / Q000235:genetics* / Q000276:immunology*; D011994:Recombinant Proteins / Q000276:immunology; D017386:Sequence Homology, Amino Acid
D018840:HSP70 Heat-Shock Proteins; D011994:Recombinant Proteins