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Common antiviral cytotoxic t-lymphocyte epitope for diverse arenaviruses

Academic Article
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Overview

authors

  • Oldstone, Michael
  • Lewicki, H.
  • Homann, D.
  • Nguyen, C.
  • Julien, S.
  • Gairin, J. E.

publication date

  • July 2001

journal

  • Journal of Virology  Journal

abstract

  • Members of the Arenaviridae family have been isolated from mammalian hosts in disparate geographic locations, leading to their grouping as Old World types (i.e., lymphocytic choriomeningitis virus [LCMV], Lassa fever virus [LFV], Mopeia virus, and Mobala virus) and New World types (i.e., Junin, Machupo, Tacaribe, and Sabia viruses) (C. J. Peters, M. J. Buchmeier, P. E. Rollin, and T. G. Ksiazek, p. 1521-1551, in B. N. Fields, D. M. Knipe, and P. M. Howley [ed.], Fields virology, 3rd ed., 1996; P. J. Southern, p. 1505-1519, in B. N. Fields, D. M. Knipe, and P. M. Howley [ed.], Fields virology, 3rd ed., 1996). Several types in both groups-LFV, Junin, Machupo, and Sabia viruses-cause severe and often lethal human diseases. By sequence comparison, we noted that eight Old World and New World arenaviruses share several amino acids with the nucleoprotein (NP) that consists of amino acids (aa) 118 to 126 (NP 118-126) (RPQASGVYM) of LCMV that comprise the immunodominant cytotoxic T-lymphocyte (CTL) epitope for H-2(d) mice (32). This L(d)-restricted epitope constituted >97% of the total bulk CTLs produced in the specific antiviral or clonal responses of H-2(d) BALB mice. NP 118-126 of the Old World arenaviruses LFV, Mopeia virus, and LCMV and the New World arenavirus Sabia virus bound at high affinity to L(d). The primary H-2(d) CTL anti-LCMV response as well as that of a CTL clone responsive to LCMV NP 118-126 recognized target cells coated with NP 118-126 peptides derived from LCMV, LFV, and Mopeia virus but not Sabia virus, indicating that a common functional NP epitope exists among Old World arenaviruses. Use of site-specific amino acid exchanges in the NP CTL epitope among these arenaviruses identified amino acids involved in major histocompatibility complex binding and CTL recognition.

subject areas

  • Amino Acid Substitution
  • Animals
  • Arenavirus
  • Epitopes, T-Lymphocyte
  • Histocompatibility Antigens
  • Mice
  • Mice, Inbred BALB C
  • Mice, Inbred C57BL
  • Nucleocapsid Proteins
  • Peptides
  • Sequence Homology, Amino Acid
  • T-Lymphocytes, Cytotoxic
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Identity

International Standard Serial Number (ISSN)

  • 0022-538X

Digital Object Identifier (DOI)

  • 10.1128/jvi.75.14.6273-6278.2001

PubMed ID

  • 11413293
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Additional Document Info

start page

  • 6273

end page

  • 6278

volume

  • 75

issue

  • 14

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