Structural models for the protein family characterized by gamete surface protein Pfs230 of Plasmodium falciparum.

By D. Gerloff, A. Creasey, Siarhei Maslau, R. Carter. 2005

138 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology, Public Health, Environmental and Occupational Health

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In Immunology

1. P. Duffy
2. Stefan H. I. Kappe

In Molecular Biology

1. L. Aravind
2. G. Clore
3. L. Miller
4. Szymon Kaczanowski
5. D. Anderson
6. Y. Takayama
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8. N. MacDonald

In Public Health, Environmental and Occupational Health

1. P. Duffy
2. Stefan H. I. Kappe
3. Silvia A. Arredondo

Citations in the corpus

• Plasmodium 6-Cysteine Proteins: Functional Diversity, Transmission-Blocking Antibodies and Structural Scaffolds (2022, background): “org 9 parallel and antiparallel b-strands and contains up to six cysteines that form disulfide bonds, where cysteines C1–C2, C3–C6, C4–C5 are connected (Figure 2A) (Gerloff et al., 2005; Arredondo et al., 2012).”
• Three Members of the 6-cys Protein Family of Plasmodium Play a Role in Gamete Fertility (2010, background): “We obtained the single nucleotide polymorphisms (SNPs) data identified from field and laboratory isolates of P. falciparum (excluding all P. reichenowi SNPs) from PlasmoDB (www.PlasmoDB.org).”
• Identification of domains within Pfs230 that elicit transmission blocking antibody responses (2019, methodology): “Out of the 30, only five protein fragments with CM domain 1 (aa 589–730)) [20] (Supplementary Table 1 and Fig.”
• N-Terminal Prodomain of Pfs230 Synthesized Using a Cell-Free System Is Sufficient To Induce Complement-Dependent Malaria Transmission-Blocking Activity (2011, background): “1A) (6, 11, 36) and elicits a humoral immune response in infected individuals that can mediate transmission-blocking immunity (12, 16).”
• Worldwide sequence conservation of transmission-blocking vaccine candidate Pvs230 in Plasmodium vivax (2011, background): “In contrast, antigens expressed in the sexualand mosquito-stages show limited polymorphism; these include Pfs25 [9], Pfs28 [32], Pfs230 [17,33,34], Pvs25 and Pvs28 [35,36].”
• Structural and Biochemical Characterization of Plasmodium falciparum 12 (Pf12) Reveals a Unique Interdomain Organization and the Potential for an Antiparallel Arrangement with Pf41* (2013, background): “The Plasmodium s48/45 domains were previously predicted to adopt a fold similar to the coccidian SRS proteins despite showing only 5–9% primary sequence identity (4).”
• Structure of the malaria vaccine candidate Pfs48/45 and its recognition by transmission blocking antibodies (2022, background): “from three domains, with N- and C-terminal 6-cys domains joined by a central 4-cys domain, all linked to the gamete membrane through a C-terminal GPI anchor [22-24].”
• Transmission-Blocking Vaccines: Harnessing Herd Immunity for Malaria Elimination (2021, background): “Preclinical studies indicate that Pfs230 immunogens that contain the N terminal region (aa 443–1132) [36], and specifically the first (Domain 1, aa 589–730 [37]) of its 14 6-cys domains [38], can induce functional antibodies.”
• Structural and Immunological Characterization of Recombinant 6-Cysteine Domains of the Plasmodium falciparum Sexual Stage Protein Pfs230* (2016, unknown): “initially modeled by Gerloff et al (24).”
• The s48/45 six-cysteine proteins: mediators of interaction throughout the Plasmodium life cycle (2016, background): “P12 has two 6-cysteine motifs similar to those detected in Pfs230 and it was deemed to be the structural archetype of the family (Williamson et al., 1993; Carter et al., 1995; Gerloff et al., 2005); its NMR analysis provided the first experimentally determined molecular structure for the 6-cys famil”
• Structure of the Pf12 and Pf41 heterodimeric complex of Plasmodium falciparum 6-cysteine proteins (2022, background): “The 6-cys domain consists of a β-sandwich fold formed by two β-sheets of mixed parallel and anti-parallel β-strands, with up to six positionally conserved cysteines that form disulfide bonds (Carter et al. 1995, Gerloff et al. 2005, Arredondo et al. 2012).”
• Structure of the Plasmodium 6-cysteine s48/45 domain (2012, background): “Overall, comparison of the structure of Pf12D2 to theD1 domain of SAG1,D2 of SporoSAG, and D1 of BSR4 (Fig.”