1921
Volume 55, Issue 5
  • ISSN: 0002-9637
  • E-ISSN: 1476-1645
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Abstract

Abstract

We have isolated a 70-kD heat-shock protein (hsp-70) cDNA from . A cDNA clone encoding the hsp-70 was isolated and sequenced, demonstrating that it is highly homologous with other 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 and assessed for antigenicity with antiserum from mice immunized with sonicated extracts of . Antigenic sites map to regions that include the two hydrophilic domains.

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/content/journals/10.4269/ajtmh.1996.55.570
1996-11-01
2017-11-21
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