Predicted disulfide-bonded structures for three uniquely related proteins of Plasmodium falciparum, Pfs230, Pfs4845 and Pf12

Carter, Richard; Coulson, Andrew; Bhatti, Sunita; Taylor, Brian J.; Elliott, John F.

doi:10.1016/0166-6851(94)00054-q

Cited by 94 publications

(91 citation statements)

References 10 publications

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“…More recently, fold recognition-based proposals regarding the catalytic mechanisms of the insecticide-transforming bacterial protein LinA (18) and the DNA repair enzyme AlkB (19) have been published alongside experimental evidence corroborating these predictions (18,20,21). Here, we present a computational prediction of the structures of Ps230-like proteins that independently supports the disulfide-bonding organization proposed by Carter et al (12), whilst it is itself supported by the structural organization proposed independently in the same report. The closest competitors to SAG1 in our initial fold analysis were two structures adopting the well described Ig fold, of the two N-terminal domains of intercellular adhesion molecules 1 and 2, respectively (PDB ID codes 1IAM and 1ZXQ; summed 3D-JURY scores are 17.0 and 15.4).…”

supporting

confidence: 80%

“…The primary structure of proteins in the Ps230 family is characterized by a unique pattern of conserved cysteine residues (here, termed Cys positions) defined by a repeated pattern of associated, strongly conserved amino acid motifs (12). Interspersed between the short motif regions are substantial regions of very divergent sequence ranging in length from 7 to 160 aa.…”

mentioning

confidence: 99%

“…Interspersed between the short motif regions are substantial regions of very divergent sequence ranging in length from 7 to 160 aa. In 1995, Carter et al (12) proposed that the Ps230 proteins are built up of unit domains and predicted a conserved set of disulfide bonds within each domain. According to this postulate, the conserved Cys positions form bridges between the following pairs: Cys 1 and 2, Cys 3 and 6, and Cys 4 and 5 (as in the cartoon representing Pf12 in Fig.…”

mentioning

confidence: 99%

“…The repeating unit found in these proteins shows the characteristics of a double domain consisting of two structurally similar parts with distinct characteristics (12). The two parts are termed A-and B-type domains in Fig.…”

mentioning

confidence: 99%

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Structural models for the protein family characterized by gamete surface protein Pfs230 ofPlasmodium falciparum

Gerloff

Creasey

Maslau

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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Ps230 is the largest representative of a 10-member family of proteins found in all Plasmodium species. The family is defined by partially conserved, cysteine-rich double domains that are Ϸ350 aa in length and have one to three predicted disulfide bridges in each half. In Plasmodium falciparum, the most dangerous human malaria, Pf12 is the smallest member of the family, comprising just one double domain. Pfs230, with 7 double domains, and Pfs48͞45 and Pfs47, with 1.5 double domains each, are found on the gamete surfaces and are thus potential candidates for a transmissionblocking vaccine. Fold prediction analyses of the double domains in Pfs230 reveal structural resemblance to SAG1 (surface antigen 1), a surface protein with a double ␤-sandwich structure from another apicomplexan parasite, Toxoplasma gondii. Template-directed modeling onto SAG1 clearly establishes the structural link between SAG1 and Pfs230 and produces positions for the cysteines that accord with the disulfide-bonding arrangement predicted for the Pfs230 family in earlier work. A highly clustered region of polymorphisms within the second double domain in Pfs230 maps to one side of the sandwich surface. This observation suggests that this region may be functional and reinforces the validity of these molecular models for the core domains of the Pfs230 family of proteins.malaria ͉ protein structure prediction ͉ fertilization ͉ fold recognition ͉ transmission-blocking vaccine target

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supporting

confidence: 80%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Structural models for the protein family characterized by gamete surface protein Pfs230 ofPlasmodium falciparum

Gerloff

Creasey

Maslau

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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120

180

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“…Each domain typically contains 6 cysteines, likely paired in disulfide bridges, which is reminiscent of other cysteine-rich apicomplexan domains such as the COWP protein family of the oocyst wall in coccidians [26,27]; the 6-Cys family that includes the Plasmodium gamete proteins Pfs230, Pfs47 and Pfs48/45 [28][29][30][31]; and the Toxoplasma SAG proteins [28,30,31]. The cpw-wpc gene family is widely conserved among apicomplexans, including Table 3).…”

Section: Cpw-wpc Proteins Are Composed Of Arrays Of a Domain Conservementioning

confidence: 99%

Translational repression of the cpw-wpc gene family in the malaria parasite Plasmodium

Rao

Santos

Pain³

et al. 2016

Parasitology International

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Please cite this article as: Rao Pavitra N., Santos Jorge M., Pain Arnab, Templeton Thomas J., Mair Gunnar R., Translational repression of the cpw-wpc gene family in the malaria parasite Plasmodium, Parasitology International (2016), doi: 10.1016/j.parint.2016 This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

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Plasmodium reichenowi:Deduced Amino Acid Sequence of Sexual Stage-Specific Surface Antigen Prs48/45and Comparison with Its Homologue inPlasmodium falciparum

Milek

Kocken

Kaan

et al. 1997

Experimental Parasitology

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Predicted disulfide-bonded structures for three uniquely related proteins of Plasmodium falciparum, Pfs230, Pfs4845 and Pf12

Cited by 94 publications

References 10 publications

Structural models for the protein family characterized by gamete surface protein Pfs230 ofPlasmodium falciparum

Structural models for the protein family characterized by gamete surface protein Pfs230 ofPlasmodium falciparum

Translational repression of the cpw-wpc gene family in the malaria parasite Plasmodium

Plasmodium reichenowi:Deduced Amino Acid Sequence of Sexual Stage-Specific Surface Antigen Prs48/45and Comparison with Its Homologue inPlasmodium falciparum

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