|
|
 Previous Article | Table of Contents | Next Article 
Blood, 1 April 2002, Vol. 99, No. 7, pp. 2477-2482
IMMUNOBIOLOGY
Expression of ABO or related antigenic carbohydrates on viral
envelopes leads to neutralization in the presence of serum
containing specific natural antibodies and complement
Andrew F. Preece,
Karen M. Strahan,
James Devitt,
Fumi-ichiro Yamamoto, and
Kenth Gustafsson
From the Molecular Immunology Unit, Institute of Child
Health, University College London, United Kingdom, and The Burnham
Institute, La Jolla, CA.
No definitive biologic function has been associated with the human
ABO histo-blood group polymorphism, or any other terminal carbohydrate
differences within or between closely related species. We have
experimentally addressed the question of whether viral particles can
become glycosylated as determined by the glycosylation (eg, ABO) status
of the producer cell and as a result be affected by human serum
containing specific natural antibodies (NAbs). Measles virus was
produced in cells transfected with cDNA encoding, either human
A-transferase, B-transferase, an inactive "O-transferase," or a pig
 1-3galactosyltransferase (1-3GT) synthesizing the Gal1-3Gal structure. The viruses were shown to carry the same ABO structures as
the cells; that is, A but not B if produced in A-type cells, and B but
not A if produced in B-type cells. Only O was detected on the virus
produced from O-type cells, whereas reduced amounts of O appeared on
the A- and B-type viral particles. In addition, the Gal1-3Gal
structure was transferred onto measles only when grown in human cells
expressing this structure. When subjected to human preimmune sera, the
A-type, the B-type, and the Gal1-3Gal viral particles were partially
neutralized in a complement-dependent manner. However, the O-type or
the Gal1-3Gal-negative viral particles were not neutralized. The
neutralization appeared to be mediated by specific NAb, as judged by
specific inhibition using synthetic A and Gal1-3Gal
oligosaccharides. Such viral glycosylation may thus partly explain why
the ABO antigens and other similar intraspecies as well as interspecies
polymorphic carbohydrates have evolved and been maintained over long
evolutionary periods.
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati What's this?
This article has been cited by other articles:
|
|
|
|
 
P. Guillon, M. Clement, V. Sebille, J.-G. Rivain, C.-F. Chou, N. Ruvoen-Clouet, and J. Le Pendu
Inhibition of the interaction between the SARS-CoV Spike protein and its cellular receptor by anti-histo-blood group antibodies
Glycobiology,
December 1, 2008;
18(12):
1085 - 1093.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J. R. Bishop and P. Gagneux
Evolution of carbohydrate antigens--microbial forces shaping host glycomes?
Glycobiology,
May 1, 2007;
17(5):
23R - 34R.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. J. D. Neil, A. McKnight, K. Gustafsson, and R. A. Weiss
HIV-1 incorporates ABO histo-blood group antigens that sensitize virions to complement-mediated inactivation
Blood,
June 15, 2005;
105(12):
4693 - 4699.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
