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Nonneutralizing antibodies binding to the surface glycoprotein of lymphocytic choriomeningitis virus reduce early virus spread

Academic Article
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Overview

authors

  • Hangartner, Lars
  • Zellweger, R. M.
  • Giobbi, M.
  • Weber, J.
  • Eschli, B.
  • McCoy, K. D.
  • Harris, N.
  • Recher, M.
  • Zinkernagel, R. M.
  • Hengartner, H.

publication date

  • August 2006

journal

  • Journal of Experimental Medicine  Journal

abstract

  • The biological relevance of nonneutralizing antibodies elicited early after infection with noncytopathic persistence-prone viruses is unclear. We demonstrate that cytotoxic T lymphocyte-deficient TgH(KL25) mice, which are transgenic for the heavy chain of the lymphocytic choriomeningitis virus (LCMV)-neutralizing monoclonal antibody KL25, mount a focused neutralizing antibody response following LCMV infection, and that this results in the emergence of neutralization escape virus variants. Further investigation revealed that some of the escape variants that arose early after infection could still bind to the selecting antibody. In contrast, no antibody binding could be detected for late isolates, indicating that binding, but nonneutralizing, antibodies exerted a selective pressure on the virus. Infection of naive TgH(KL25) mice with distinct escape viruses differing in their antibody-binding properties revealed that nonneutralizing antibodies accelerated clearance of antibody-binding virus variants in a partly complement-dependent manner. Virus variants that did not bind antibodies were not affected. We therefore conclude that nonneutralizing antibodies binding to the same antigenic site as neutralizing antibodies are biologically relevant by limiting early viral spread.

subject areas

  • Animals
  • Antibodies, Viral
  • Antigens, Viral
  • B-Lymphocytes
  • Binding Sites, Antibody
  • Complement Activation
  • Glycoproteins
  • Lymphocytic Choriomeningitis
  • Lymphocytic choriomeningitis virus
  • Membrane Glycoproteins
  • Mice
  • Mice, Inbred C57BL
  • Neutralization Tests
  • Recombinant Proteins
  • T-Lymphocytes, Cytotoxic
  • Viral Proteins
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Identity

PubMed Central ID

  • PMC2118372

International Standard Serial Number (ISSN)

  • 0022-1007

Digital Object Identifier (DOI)

  • 10.1084/jem.20051557

PubMed ID

  • 16880253
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Additional Document Info

start page

  • 2033

end page

  • 2042

volume

  • 203

issue

  • 8

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