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Originally published In Press as doi:10.1074/jbc.M207145200 on September 18, 2002
J. Biol. Chem., Vol. 277, Issue 49, 47533-47540, December 6, 2002
Serine Repeat Antigen (SERA5) Is Predominantly
Expressed among the SERA Multigene Family of Plasmodium
falciparum, and the Acquired Antibody Titers Correlate with Serum
Inhibition of the Parasite Growth*
Sayaka
Aoki ,
Jie
Li ,
Sawako
Itagaki ,
Brenda A.
Okech§,
Thomas G.
Egwang§,
Hiroyuki
Matsuoka¶,
Nirianne Marie Q.
Palacpac ,
Toshihide
Mitamura , and
Toshihiro
Horii
From the Department of Molecular Protozoology,
Research Institute for Microbial Diseases, Osaka University, Suita,
Osaka 565-0871, Japan, the § Division of Medical
Parasitology and Tropical Medicine, Med Biotech Laboratories, Kampala,
Uganda, and ¶ Department of Medical Zoology, Jichi Medical School,
3311-1 Yakushiji, Minamikawachi-machi, Kawachi-gun,
Tochigi 329-0498, Japan
The Plasmodium falciparum serine
repeat antigen (SERA) is one of the blood stage malaria vaccine
candidates. The malaria genome project has revealed that SERA is a
member of the SERA multigene family consisting of eight SERA homologues
clustered on chromosome 2 and one SERA homologue on chromosome 9. Northern blotting and real time quantitative reverse
transcription-PCR with five independent parasite strains,
including three allelic representative forms of the SERA gene, have
shown that all of the SERA homologues are transcribed most actively at
trophozoite and schizont stages and that SERA5 (SERA/SERP) is
transcribed predominantly among the family. Polyclonal antibodies were
raised against recombinant proteins representing the N-terminal
portions of four significantly transcribed SERA homologues (SERA3 to
-6) in the center of the cluster on chromosome 2. Using these
antibodies, indirect immunofluorescence microscopy detected the
expression of SERA3 to -6, with similar localization, in all
trophozoite- and schizont-infected erythrocytes. We have examined 40 sera from Ugandan adults for their antibody reactivity and found that
enzyme-linked immunosorbent assay titer against SERA5 N-terminal
domain, but not against other SERA proteins, is positively
correlated with the inhibition of in vitro parasite growth by individual sera. Our data confirm the usefulness of the
N-terminal domain of SERA5 as a promising malaria candidate vaccine.
*
This work was supported by Grant-in-Aid for Scientific
Research (A) 13357002 and Grant-in-Aid for Scientific Research on
Priority Areas 13226058 (to T. H.) from the Ministry of Education,
Science, Sports, Culture, and Technology of Japan. This work also
received financial support from the United Nations Developmental
Program/World Bank/World Health Organization/Special Program for
Research and Training in Tropical Diseases (TDR).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
81-6-68798280; Fax: 81-6-68798281; E-mail:
horii@biken.osaka-u.ac.jp.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.
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