Antigenic properties of human parechovirus 1

被引:50
作者
Joki-Korpela, P
Roivainen, M
Lankinen, H
Pöyry, T
Hyypiä, T
机构
[1] Univ Helsinki, Dept Virol, Haartman Inst, FIN-00014 Helsinki, Finland
[2] Univ Turku, Dept Virol, FIN-20520 Turku, Finland
[3] Univ Turku, MediCity Res Labs, FIN-20520 Turku, Finland
[4] Natl Publ Hlth Inst, Enterovirus Lab, FIN-00300 Helsinki, Finland
关键词
D O I
10.1099/0022-1317-81-7-1709
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Human parechoviruses 1 and 2 (HPEV1 and HPEV2, respectively), formerly known as echoviruses 22 and 23, have been assigned to a novel picornavirus genus on the basis of their distinct molecular and biological properties. To study the immunological characteristics of HPEV1 capsid proteins, antigenic analysis was carried out by a peptide scanning technique, which can be used to identify the immunogenic peptide sequences of a protein. Partially overlapping peptides, representing the capsid of HPEV1, were synthesized using a 12 aa window in a three residue shift and reactivity of rabbit and murine HPEV1 antisera against these peptides were tested. Using this method, an antigenic site in the VPO polypeptide, recognized by both rabbit and murine antisera, was identified. The sequence of this region was conserved among HPEV1 clinical isolates obtained from Finland and the United States. Antiserum against this peptide region showed neutralizing activity against HPEV1 in cell culture. Because the C-terminal region of HPEV1 VP1 contains a functional RGD motif, the antigenicity of this region was also tested. By using the corresponding peptide antiserum, neutralization of HPEV1 was observed, Cross-neutralization between HPEV1 and coxsackievirus A9, an enterovirus with a similar RGD motif in VP1, was also detected.
引用
收藏
页码:1709 / 1718
页数:10
相关论文
共 53 条
  • [1] MANY RHINOVIRUS SEROTYPES SHARE THE SAME CELLULAR RECEPTOR
    ABRAHAM, G
    COLONNO, RJ
    [J]. JOURNAL OF VIROLOGY, 1984, 51 (02) : 340 - 345
  • [2] THE 3-DIMENSIONAL STRUCTURE OF FOOT-AND-MOUTH-DISEASE VIRUS AT 2.9-A RESOLUTION
    ACHARYA, R
    FRY, E
    STUART, D
    FOX, G
    ROWLANDS, D
    BROWN, F
    [J]. NATURE, 1989, 337 (6209) : 709 - 716
  • [3] NEUTRALIZATION EPITOPES OF HUMAN RHINOVIRUS TYPE-2
    APPLEYARD, G
    RUSSELL, SM
    CLARKE, BE
    SPELLER, SA
    TROWBRIDGE, M
    VADOLAS, J
    [J]. JOURNAL OF GENERAL VIROLOGY, 1990, 71 : 1275 - 1282
  • [4] THE NUCLEOTIDE-SEQUENCES OF WILD-TYPE COXSACKIEVIRUS-A9 STRAINS IMPLY THAT AN RGD MOTIF IN VP1 IS FUNCTIONALLY SIGNIFICANT
    CHANG, KH
    DAY, C
    WALKER, J
    HYYPIA, T
    STANWAY, G
    [J]. JOURNAL OF GENERAL VIROLOGY, 1992, 73 : 621 - 626
  • [5] AN OUTBREAK OF ACUTE FLACCID PARALYSIS IN JAMAICA ASSOCIATED WITH ECHOVIRUS TYPE-22
    FIGUEROA, JP
    ASHLEY, D
    KING, D
    HULL, B
    [J]. JOURNAL OF MEDICAL VIROLOGY, 1989, 29 (04) : 315 - 319
  • [6] THE CELL ATTACHMENT SITE ON FOOT-AND-MOUTH-DISEASE VIRUS INCLUDES THE AMINO-ACID SEQUENCE RGD (ARGININE-GLYCINE-ASPARTIC ACID)
    FOX, G
    PARRY, NR
    BARNETT, PV
    MCGINN, B
    ROWLANDS, DJ
    BROWN, F
    [J]. JOURNAL OF GENERAL VIROLOGY, 1989, 70 : 625 - 637
  • [7] SPOT-SYNTHESIS - AN EASY TECHNIQUE FOR THE POSITIONALLY ADDRESSABLE, PARALLEL CHEMICAL SYNTHESIS ON A MEMBRANE SUPPORT
    FRANK, R
    [J]. TETRAHEDRON, 1992, 48 (42) : 9217 - 9232
  • [8] Molecular analysis of human parechovirus type 2 (formerly echovirus 23)
    Ghazi, F
    Hughes, PJ
    Hyypiä, T
    Stanway, G
    [J]. JOURNAL OF GENERAL VIROLOGY, 1998, 79 : 2641 - 2650
  • [9] Grist N R, 1978, Prog Med Virol, V24, P114
  • [10] The crystal structure of coxsackievirus A9:: new insights into the uncoating mechanisms of enteroviruses
    Hendry, E
    Hatanaka, H
    Fry, E
    Smyth, M
    Tate, J
    Stanway, G
    Santti, J
    Maaronen, M
    Hyypiä, T
    Stuart, D
    [J]. STRUCTURE WITH FOLDING & DESIGN, 1999, 7 (12): : 1527 - 1538