Identification and cloning of a locus of serine repeat antigen (sera)-related genes from Plasmodium vivax

Kiefer, Michael; Crawford, Kenneth A.; Boley, Leslie J.; Landsberg, Katherine E.; Gibson, Helen L.; Kaslow, David C.; Barr, Philip J.

doi:10.1016/s0166-6851(96)02607-2

Cited by 29 publications

(13 citation statements)

References 33 publications

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“…SERA homologs were identified in other Plasmodium species. Kiefer et al (1996) found five SERA genes from another human parasite, P. vivax and Gor et al (1998) identified three SERA genes from the rodent parasite of P. vinckei. Completed or ongoing genome projects of eight Plasmodium species: two human malaria parasites, P. falciparum and P. vivax; chimpanzee parasite P. reichenowi; macaque parasite P. knowlesi; three rodent parasites P. berghei, P. yoelii and P. chabaudi; and avian parasite P. gallinaceum, confirmed the gene organization and allowed phylogenetic analysis of the SERA gene family (Burgon et al, 2005;Arisue et al, 2007).…”

Section: Research History Of the Sera Multigene Familymentioning

confidence: 99%

“…For more than 10 years after the first description of a gene family member, the existence of the Plasmodium serine repeat antigen (SERA) multigene family has been overlooked. Serine repeat antigen family proteins share homology with the papain family of cysteine proteases (Kiefer et al, 1996;Gor et al, 1998;Bourgon et al, 2004;Arisue et al, 2007Arisue et al, , 2011. Almost all SERA genes are clustered in a head-to-tail manner and the number of SERA genes in the clustered region varies among parasite species (Bourgon et al, 2004;McCoubrie et al, 2007;Arisue et al, 2007Arisue et al, , 2011.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Clues to Evolution of the SERA Multigene Family in the Genus Plasmodium

Arisue¹,

Palacpac²,

Tanabe³

et al. 2011

Gene Duplication

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Section: Research History Of the Sera Multigene Familymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Clues to Evolution of the SERA Multigene Family in the Genus Plasmodium

Arisue¹,

Palacpac²,

Tanabe³

et al. 2011

Gene Duplication

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“…The C-terminal end of the central domain of all SERA proteins shows approximately 20% sequence identity to the papain family of cysteine proteases (8,18,23). Curiously, six of the nine P. falciparum SERAs (SERA1 to -5 and SERA9) have a cysteine-to-serine replacement within the putative catalytic triad; the remaining three SERAs (SERA6 to -8) have the canonical cysteine as the active-site residue.…”

mentioning

confidence: 99%

Inhibition of Malaria Parasite Development by a Cyclic Peptide That Targets the Vital Parasite Protein SERA5

et al. 2008

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The serine repeat antigen (SERA) proteins of the malaria parasites Plasmodium spp. contain a putative enzyme domain similar to that of papain family cysteine proteases. In Plasmodium falciparum parasites, more than half of the SERA family proteins, including the most abundantly expressed form, SERA5, have a cysteine-to-serine substitution within the putative catalytic triad of the active site. Although SERA5 is required for blood-stage parasite survival, the occurrence of a noncanonical catalytic triad casts doubt on the importance of the enzyme domain in this function. We used phage display to identify a small (14-residue) disulfidebonded cyclic peptide (SBP1) that targets the enzyme domain of SERA5. Biochemical characterization of the interaction shows that it is dependent on the conformation of both the peptide and protein. Addition of this peptide to parasite cultures compromised development of late-stage parasites compared to that of control parasites or those incubated with equivalent amounts of the carboxymethylated peptide. This effect was similar in two different strains of P. falciparum as well as in a transgenic strain where the gene encoding the related serine-type parasitophorous vacuole protein SERA4 was deleted. In compromised parasites, the SBP1 peptide crosses both the erythrocyte and parasitophorous vacuole membranes and accumulates within the parasitophorous vacuole. In addition, both SBP1 and SERA5 were identified in the parasite cytosol, indicating that the plasma membrane of the parasite was compromised as a result of SBP1 treatment. These data implicate an important role for SERA5 in the regulation of the intraerythrocytic development of late-stage parasites and as a target for drug development.

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“…A number of SERA homologues have been described, namely serine repeat protein homologue (SERPH [9] or SERA-2 [10]) and SERA-3 [10] from P. falciparum and five homologues from Plasmodium 6i6ax [11]. SERA and SERPH have been localized to the parasitophorous vacuole of mature schizonts [9,12], and SERA fragments are released into the bloodstream near the time of erythrocyte rupture [12].…”

mentioning

confidence: 99%

“…Our comparison of the protease domains of described SERA homologues (the sequence of the SERA-3 protease domain is not available) identified two subclasses of proteins, represented by P. falciparum SERA and SERPH ( Table 1). The SERA subclass includes SERA, five previously described P. 6i6ax proteins ( [11]; SERA vivax 1-5) and SERA vinckei -3. These proteins share 55% identity in their protease domains.…”

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confidence: 99%

Plasmodial serine repeat antigen homologues with properties of schizont cysteine proteases

Gor

Wiser

et al. 1998

Molecular and Biochemical Parasitology

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Proteases appear to be required for critical events in the erythrocytic life cycle of malaria parasites, including the rupture of erythrocytes by mature schizonts and the subsequent invasion of erythrocytes by daughter merozoites [1,2]. This conclusion is supported by studies showing that parasite rupture and invasion of erythrocytes are inhibited by serine and cysteine protease inhibitors [1] and that the proteolytic processing of late schizont-stage proteins is required for the completion of the erythrocytic cycle [3,4]. A number of schizont protease activities have been identified biochemically [2], but limitations on available quantities of protein have made it difficult to definitively characterize these proteases or to ascertain their specific biological roles.The Plasmodium falciparum serine repeat antigen (known as SERA, SERA-1, SERP or P126 [5][6][7]) is being studied as a potential vaccine component [8]. A number of SERA homologues have been described, namely serine repeat protein homologue (SERPH [9] or SERA-2 [10]) and SERA-3 [10] from P. falciparum and five homologues from Plasmodium 6i6ax [11]. SERA and SERPH have been localized to the parasitophorous vacuole of mature schizonts [9,12], and SERA fragments are released into the bloodstream near the time of erythrocyte rupture [12]. SERA and its homologues all contain a 30 kDa 'protease domain' that has similarity in sequence to papain-family cysteine proteases, particularly near highly conserved active site residues [13] (Fig. 1A). Taken together, available data suggest that SERA and SERPH may act as late schizontAbbre6iations: SERA, serine repeat antigen; SERPH, serine repeat antigen homologue.

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Identification and cloning of a locus of serine repeat antigen (sera)-related genes from Plasmodium vivax

Cited by 29 publications

References 33 publications

Clues to Evolution of the SERA Multigene Family in the Genus Plasmodium

Clues to Evolution of the SERA Multigene Family in the Genus Plasmodium

Inhibition of Malaria Parasite Development by a Cyclic Peptide That Targets the Vital Parasite Protein SERA5

Plasmodial serine repeat antigen homologues with properties of schizont cysteine proteases

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