Coupling Peptide Antigens to Virus-Like Particles or to Protein Carriers Influences the Th1/Th2 Polarity of the Resulting Immune Response

被引:17
作者
Pomwised, Rattanaruji [1 ]
Intamaso, Uraiwan [2 ]
Teintze, Martin [3 ]
Young, Mark [4 ]
Pincus, Seth H. [5 ]
机构
[1] Prince Songkla Univ, Sch Med, Dept Microbiol, Hat Yai 90110, Thailand
[2] Burapha Univ, Fac Allied Hlth Sci, Chon Buri 20131, Thailand
[3] Montana State Univ, Dept Chem & Biochem, Bozeman, MT 59717 USA
[4] Montana State Univ, Dept Plant Sci, Bozeman, MT 59717 USA
[5] Louisianna State Univ, Sch Med, Dept Pediat & Microbiol, New Orleans, LA 70118 USA
关键词
group B streptococcus; Streptococcus agalactiae; capsular polysaccharide; antigen; mimotope; synthetic peptide; COWPEA MOSAIC-VIRUS; CHIMERAS; EXPRESSION; MUTANT; CELLS;
D O I
10.3390/vaccines4020015
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
We have conjugated the S9 peptide, a mimic of the group B streptococcal type III capsular polysaccharide, to different carriers in an effort to elicit an optimal immune response. As carriers, we utilized the soluble protein keyhole limpet hemocyanin and virus-like particles (VLPs) from two plant viruses, Cowpea Chlorotic Mottle Virus and Cowpea Mosaic Virus. We have found that coupling the peptide to the soluble protein elicits a Th2 immune response, as evidenced by the production of the peptide-specific IgG1 antibody and IL-4/IL-10 production in response to antigen stimulation, whereas the peptide conjugated to VLPs elicited a Th1 response (IgG2a, IFN-). Because the VLPs used as carriers package RNA during the assembly process, we hypothesize that this effect may result from the presence of nucleic acid in the immunogen, which affects the Th1/Th2 polarity of the response.
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页数:10
相关论文
共 19 条
[1]   DESIGN AND CONSTRUCTION OF RHINOVIRUS CHIMERAS INCORPORATING IMMUNOGENS FROM POLIO, INFLUENZA, AND HUMAN IMMUNODEFICIENCY VIRUSES [J].
ARNOLD, GF ;
RESNICK, DA ;
LI, YL ;
ZHANG, AQ ;
SMITH, AD ;
GEISLER, SC ;
JACOBOMOLINA, A ;
LEE, WM ;
WEBSTER, RG ;
ARNOLD, E .
VIROLOGY, 1994, 198 (02) :703-708
[2]   Influenza virus-like particles elicit broader immune responses than whole virion inactivated influenza virus or recombinant hemagglutinin [J].
Bright, Rick A. ;
Carter, Donald M. ;
Daniluk, Shannon ;
Toapanta, Franklin R. ;
Ahmad, Attiya ;
Gavrilov, Victor ;
Massare, Mike ;
Pushko, Peter ;
Mytle, Nutan ;
Rowe, Thomas ;
Smith, Gale ;
Ross, Ted M. .
VACCINE, 2007, 25 (19) :3871-3878
[3]   Heterologous expression of the modified coat protein of Cowpea chlorotic mottle bromovirus results in the assembly of protein cages with altered architectures and function [J].
Brumfield, S ;
Willits, D ;
Tang, L ;
Johnson, JE ;
Douglas, T ;
Young, M .
JOURNAL OF GENERAL VIROLOGY, 2004, 85 :1049-1053
[4]   ANTIGEN CHIMERAS OF POLIOVIRUS AS POTENTIAL NEW VACCINES [J].
BURKE, KL ;
DUNN, G ;
FERGUSON, M ;
MINOR, PD ;
ALMOND, JW .
NATURE, 1988, 332 (6159) :81-82
[5]   Immunogenicity of papaya mosaic virus-like particles fused to a hepatitis C virus epitope: Evidence for the critical function of multimerization [J].
Denis, Jerome ;
Majeau, Nathalie ;
Acosta-Ramirez, Elizabeth ;
Savard, Christian ;
Bedard, Marie-Claude ;
Simard, Sabrina ;
Lecours, Katia ;
Bolduc, Marilene ;
Pare, Christine ;
Willems, Bernard ;
Shoukry, Naglaa ;
Tessier, Philippe ;
Lacasse, Patrick ;
Lamarre, Alain ;
Lapointe, Rjean ;
Lopez Macias, Constantino ;
Leclerc, Denis .
VIROLOGY, 2007, 363 (01) :59-68
[6]   Characterization of a disassembly deficient mutant of cowpea chlorotic mottle virus [J].
Fox, JM ;
Albert, FG ;
Speir, JA ;
Young, MJ .
VIROLOGY, 1997, 227 (01) :229-233
[7]   Analysis of a salt stable mutant of cowpea chlorotic mottle virus [J].
Fox, JM ;
Zhao, XX ;
Speir, JA ;
Young, MJ .
VIROLOGY, 1996, 222 (01) :115-122
[8]   NMR studies of carbohydrates and carbohydrate-mimetic peptides recognized by an anti-group B Streptococcus antibody [J].
Johnson, MA ;
Jaseja, M ;
Zou, W ;
Jennings, HJ ;
Copié, V ;
Pinto, BM ;
Pincus, SH .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (27) :24740-24752
[9]   Phage display mapping for peptide 11 sensitive sequences binding to laminin-1 [J].
Kazmin, DA ;
Hoyt, TR ;
Taubner, L ;
Teintze, M ;
Starkey, JR .
JOURNAL OF MOLECULAR BIOLOGY, 2000, 298 (03) :431-445
[10]  
Pincus SH, 1998, J IMMUNOL, V160, P293