Antibodies against the extracellular enveloped virus B5R protein are mainly responsible for the EEV neutralizing capacity of vaccinia immune globulin

被引:108
作者
Bell, E
Shamim, M
Whitbeck, JC
Sfyroera, G
Lambris, JD
Isaacs, SN
机构
[1] Univ Penn, Sch Med, Div Infect Dis, Dept Med, Philadelphia, PA 19104 USA
[2] Univ Penn, Sch Dent Med, Dept Microbiol, Philadelphia, PA 19104 USA
[3] Univ Penn, Sch Med, Dept Pathol & Lab Med, Philadelphia, PA 19104 USA
关键词
vaccinia virus; vaccinia immune globulin; VIG; B5R; extracellular enveloped virus; EEV; virus neutralization; vaccination complications; neutralization tests;
D O I
10.1016/j.virol.2004.05.004
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
In the event of smallpox bioterrorism, widespread vaccination may be required. Vaccinia immune globulin (VIG) has been used to treat complications from the smallpox vaccine. While the potency of VIG was defined by its ability to neutralize intracellular mature vinis, a second form of vaccinia called the extracellular enveloped virus (EEV) is critical for virus spread in the host. The B5R-protein is one of many EEV-specific proteins. Immunoprecipitation and ELISA revealed that VIG recognizes the B5R-protein. An EEV plaque-reduction assay using a recombinant vaccinia that lacks the majority of the extracellular domain of B5R showed that the ability of VIG to neutralize EEV is principally directed at B5R. In addition, absorbing out the anti-B5R antibody present in VIG through the addition of recombinant B5R protein abrogated VIG's ability to significantly neutralize wild-type EEV This work demonstrates the prominent role of B5R as a target of EEV-neutralizing activity of human antibodies. (C) 2004 Elsevier Inc. All rights reserved.
引用
收藏
页码:425 / 431
页数:7
相关论文
共 25 条
[11]   Four-gene-combination DNA vaccine protects mice against a lethal vaccinia virus challenge and elicits appropriate antibody responses in nonhuman primates [J].
Hooper, JW ;
Custer, DM ;
Thompson, E .
VIROLOGY, 2003, 306 (01) :181-195
[12]   IDENTIFICATION OF A VACCINIA VIRUS PENETRATION PROTEIN [J].
ICHIHASHI, Y ;
TAKAHASHI, T ;
OIE, M .
VIROLOGY, 1994, 202 (02) :834-843
[13]   CHARACTERIZATION OF A VACCINIA VIRUS-ENCODED 42-KILODALTON CLASS-I MEMBRANE GLYCOPROTEIN COMPONENT OF THE EXTRACELLULAR VIRUS ENVELOPE [J].
ISAACS, SN ;
WOLFFE, EJ ;
PAYNE, LG ;
MOSS, B .
JOURNAL OF VIROLOGY, 1992, 66 (12) :7217-7224
[14]  
KEMPE CH, 1956, PEDIATRICS, V18, P177
[15]   Antibody-sensitive and antibody-resistant cell-to-cell spread by vaccinia virus: role of the A33R protein in anti body-resistant spread [J].
Law, M ;
Hollinshead, R ;
Smith, GL .
JOURNAL OF GENERAL VIROLOGY, 2002, 83 :209-222
[16]   Antibody neutralization of the extracellular enveloped form of vaccinia virus [J].
Law, M ;
Smith, GL .
VIROLOGY, 2001, 280 (01) :132-142
[17]   The extracellular domain of vaccinia virus protein B5R affects plaque phenotype, extracellular enveloped virus release, and intracellular actin tail formation [J].
Mathew, E ;
Sanderson, CM ;
Hollinshead, M ;
Smith, GL .
JOURNAL OF VIROLOGY, 1998, 72 (03) :2429-2438
[19]   Functional region IV of glycoprotein D from herpes simplex virus modulates glycoprotein binding to the herpesvirus entry mediator [J].
Rux, AH ;
Willis, SH ;
Nicola, AV ;
Hou, WF ;
Peng, C ;
Lou, H ;
Cohen, GH ;
Eisenberg, RJ .
JOURNAL OF VIROLOGY, 1998, 72 (09) :7091-7098
[20]  
Smith GL, 1998, ADV EXP MED BIOL, V440, P395