Lack of gender-specific antibody recognition of products from domains of a var gene implicated in pregnancy-associated Plasmodium falciparum malaria

被引:17
作者
Jensen, ATR
Zornig, HD
Buhmann, C
Salanti, A
Koram, KA
Riley, EM
Theander, TG
Hviid, L
Staalsoe, T
机构
[1] Rigshosp, Dept Infect Dis M7641, Ctr Med Parasitol, DK-2200 Copenhagen N, Denmark
[2] Univ Copenhagen, Inst Med Microbiol & Immunol, Copenhagen, Denmark
[3] Univ Ghana, Epidemiol Unit, Noguchi Mem Inst Med Res, Legon, Ghana
[4] London Sch Hyg & Trop Med, London WC1, England
关键词
D O I
10.1128/IAI.71.7.4193-4196.2003
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Gender-specific and parity-dependent acquired antibody recognition is characteristic of variant surface antigens (VSA) expressed by chondroitin sulfate A (CSA)-adherent Plasmodium falciparum involved in pregnancy-associated malaria (PAM). However, antibody recognition of recombinant products of a specific VSA gene (2O2var1) implicated in PAM and transcribed by a CSA-adhering parasite line did not have these characteristics. Furthermore, we could not demonstrate preferential transcription of 2O2var1 in the CSA-adhering line versus the unselected, parental isolate. Our data call for circumspection regarding the molecular identity of the parasite ligand mediating adhesion to CSA in PAM.
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收藏
页码:4193 / 4196
页数:4
相关论文
共 31 条
[1]   Characterization of proteoglycans of human placenta and identification of unique chondroitin sulfate proteoglycans of the intervillous spaces that mediate the adherence of Plasmodium falciparum-infected erythrocytes to the placenta [J].
Achur, RN ;
Valiyaveettil, M ;
Alkhalil, A ;
Ockenhouse, CF ;
Gowda, DC .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (51) :40344-40356
[2]   Inhibition of binding of malaria-infected erythrocytes by a tetradecasaccharide fraction from chondroitin sulfate A [J].
Beeson, JG ;
Chai, WG ;
Rogerson, SJ ;
Lawson, AM ;
Brown, GV .
INFECTION AND IMMUNITY, 1998, 66 (07) :3397-3402
[3]  
BRABIN BJ, 1983, B WORLD HEALTH ORGAN, V61, P1005
[4]   Plasmodium falciparum domain mediating adhesion to chondroitin sulfate A:: A receptor for human placental infection [J].
Buffet, PA ;
Gamain, B ;
Scheidig, C ;
Baruch, D ;
Smith, JD ;
Hernandez-Rivas, R ;
Pouvelle, B ;
Oishi, S ;
Fujii, N ;
Fusai, T ;
Parzy, D ;
Miller, LH ;
Gysin, J ;
Scherf, A .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (22) :12743-12748
[5]   The role of antibodies to Plasmodium falciparum-infected-erythrocyte surface antigens in naturally acquired immunity to malaria [J].
Bull, PC ;
Marsh, K .
TRENDS IN MICROBIOLOGY, 2002, 10 (02) :55-58
[6]   Cytoadherence characteristics of Plasmodium falciparum isolates from Thailand: Evidence for chondroitin sulfate a as a cytoadherence receptor [J].
Chaiyaroj, SC ;
Angkasekwinai, P ;
Buranakiti, A ;
Looareesuwan, S ;
Rogerson, SJ ;
Brown, GV .
AMERICAN JOURNAL OF TROPICAL MEDICINE AND HYGIENE, 1996, 55 (01) :76-80
[7]   Plasmodium falciparum:: Cloned and expressed CIDR domains of PfEMP1 bind to chondroitin sulfate A [J].
Degen, R ;
Weiss, N ;
Beck, HP .
EXPERIMENTAL PARASITOLOGY, 2000, 95 (02) :113-121
[8]   Sequestration of Plasmodium falciparum-infected erythrocytes to chondroitin sulfate A, a receptor for maternal malaria:: monoclonal antibodies against the native parasite ligand reveal pan-reactive epitopes in placental isolates [J].
Douki, JBL ;
Traore, B ;
Costa, FTM ;
Fusaï, T ;
Pouvelle, B ;
Sterkers, Y ;
Scherf, A ;
Gysin, J .
BLOOD, 2002, 100 (04) :1478-1483
[9]   Two DBLγ subtypes are commonly expressed by placental isolates of Plasmodium falciparum [J].
Fried, M ;
Duffy, PE .
MOLECULAR AND BIOCHEMICAL PARASITOLOGY, 2002, 122 (02) :201-210
[10]   Adherence of Plasmodium falciparum to chondroitin sulfate A in the human placenta [J].
Fried, M ;
Duffy, PE .
SCIENCE, 1996, 272 (5267) :1502-1504