Antigenic and sequence diversity at the C-terminus of the merozoite surface protein-1 from rodent malaria isolates, and the binding of protective monoclonal antibodies

被引:15
作者
Benjamin, PA
Ling, IT [1 ]
Clottey, G
Valero, LMS
Ogun, SA
Fleck, SL
Walliker, D
Morgan, WD
Birdsall, B
Feeney, J
Holder, AA
机构
[1] Natl Inst Med Res, Div Parasitol, London NW7 1AA, England
[2] Natl Inst Med Res, Div Mol Struct, London NW7 1AA, England
[3] Univ Edinburgh, Inst Cell Anim & Populat Biol, Edinburgh EH9 3JT, Midlothian, Scotland
基金
英国医学研究理事会;
关键词
malaria; Plasmodium yoelii; merozoite surface protein; sequence heterogeneity;
D O I
10.1016/S0166-6851(99)00142-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Merozoite surface protein-1 (MSP-1) is a major candidate in the development of a vaccine against malaria, Immunisation with a recombinant fusion protein containing the two Plasmodium yoelii MSP-1 C-terminal epidermal growth factor-like domains (MSP-1(19)) can protect mice against homologous but not heterologous challenge, and therefore, antigenic differences resulting from sequence diversity in MSP-1,, may be crucial in determining the potential of this protein as a vaccine. Representative sequence variants from a number of distinct P. yoelii isolates were expressed in Escherichia coli and the resulting recombinant proteins were screened for binding to a panel of monoclonal antibodies (Mabs) capable of suppressing a P. yoelii YM challenge infection in passive immunisation experiments. The sequence polymorphisms affected the binding of the antibodies to the recombinant proteins. None of the Mabs recognised MSP-1(19) of P. yoelii yoelii 2CL or 33X or P, yoelii nigeriensis N67. The epitopes recognised by the Mabs were further distinguished by their reactivity with the other fusion proteins. The extent of sequence variation in MSP-1(19) among the isolates was extensive, with differences detected at 35 out of the 96 positions compared. Using the 3-dimensional structure of the Plasmodium falciparum MSP-1(19) as a model, the locations of the amino acid substitutions that may affect Mab binding were identified. The DNA sequence of MSP-1(19) from two Plasmodium vinckei isolates was also cloned and the deduced amino acid sequence compared with that in other species. (C) 1999 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:147 / 156
页数:10
相关论文
共 37 条
[1]  
Beale G.H., 1978, P213
[2]   PROTEOLYTIC PROCESSING OF THE PLASMODIUM-FALCIPARUM MEROZOITE SURFACE PROTEIN-1 PRODUCES A MEMBRANE-BOUND FRAGMENT CONTAINING 2 EPIDERMAL GROWTH FACTOR-LIKE DOMAINS [J].
BLACKMAN, MJ ;
LING, IT ;
NICHOLLS, SC ;
HOLDER, AA .
MOLECULAR AND BIOCHEMICAL PARASITOLOGY, 1991, 49 (01) :29-34
[3]   A SINGLE FRAGMENT OF A MALARIA MEROZOITE SURFACE PROTEIN REMAINS ON THE PARASITE DURING RED-CELL INVASION AND IS THE TARGET OF INVASION-INHIBITING ANTIBODIES [J].
BLACKMAN, MJ ;
HEIDRICH, HG ;
DONACHIE, S ;
MCBRIDE, JS ;
HOLDER, AA .
JOURNAL OF EXPERIMENTAL MEDICINE, 1990, 172 (01) :379-382
[4]   Plasmodium knowlesi secondary processing of the malaria merozoite surface protein-1 [J].
Blackman, MJ ;
Dennis, ED ;
Hirst, EMA ;
Kocken, CH ;
ScottFinnigan, TJ ;
Thomas, AW .
EXPERIMENTAL PARASITOLOGY, 1996, 83 (02) :229-239
[5]  
BURNS JM, 1989, J IMMUNOL, V142, P2835
[6]  
BURNS JM, 1989, J IMMUNOL, V143, P2670
[7]   MONOCLONAL-ANTIBODIES THAT INHIBIT PLASMODIUM-FALCIPARUM INVASION IN-VITRO RECOGNIZE THE 1ST GROWTH FACTOR-LIKE DOMAIN OF MEROZOITE SURFACE PROTEIN-1 [J].
CHAPPEL, JA ;
HOLDER, AA .
MOLECULAR AND BIOCHEMICAL PARASITOLOGY, 1993, 60 (02) :303-312
[8]   The crystal structure of C-terminal merozoite surface protein 1 at 1.8 Å resolution, a highly protective malaria vaccine candidate [J].
Chitarra, V ;
Holm, I ;
Bentley, GA ;
Pêtres, S ;
Longacre, S .
MOLECULAR CELL, 1999, 3 (04) :457-464
[9]   COMPARISON OF THE CARBOXY-TERMINAL, CYSTEINE-RICH DOMAIN OF THE MEROZOITE SURFACE PROTEIN-1 FROM SEVERAL STRAINS OF PLASMODIUM-YOELII [J].
DALY, TM ;
BURNS, JM ;
LONG, CA .
MOLECULAR AND BIOCHEMICAL PARASITOLOGY, 1992, 52 (02) :279-282
[10]  
DALY TM, 1995, J IMMUNOL, V155, P236