Predicted disulfide-bonded structures for three uniquely related proteins of Plasmodium falciparum, Pfs230, Pfs48/45 and Pf12.

By Richard Carter, A. Coulson, S. Bhatti, B. J. Taylor, John F. Elliott. 1995

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The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

1. Silvia A. Arredondo
2. M. Dietrich
3. Stefan H. I. Kappe
4. W. Tham
5. N. MacDonald
6. P. Duffy
7. M. V. van Dijk
8. L. Chan

Citations in the corpus

• 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”
• 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).”
• Structural and Biochemical Characterization of Plasmodium falciparum 12 (Pf12) Reveals a Unique Interdomain Organization and the Potential for an Antiparallel Arrangement with Pf41* (2013, result): “The 2-domain structure of Pf12 confirms the previous prediction for the disulfide bonding pattern of each domain (62) and is generally consistent with the original predicted strand topology based off the structure ofTgSAG1 (4).”
• Worldwide sequence conservation of transmission-blocking vaccine candidate Pvs230 in Plasmodium vivax (2011, background): “5 kb region [16,17] (Fig.”
• Three Members of the 6-cys Protein Family of Plasmodium Play a Role in Gamete Fertility (2010, background): “be Apicomplexan specific and has a predicted relationship to the SAG proteins in Toxoplasma gondii [7,8,9,10,11].”
• Transmission-Blocking Vaccines: Harnessing Herd Immunity for Malaria Elimination (2021, background): “explained in part by difficulty in generating properly folded recombinant protein: numerous disulfide bonds stabilize the structure of leading TBV antigens and make recombinant expression difficult [37,62,63].”
• Structure of the Plasmodium 6-cysteine s48/45 domain (2012, methodology): “The two tandem domains forming a pair in s48/45 proteins were respectively labeled as “A-type” and “B-type” domains in the original work defining the s48/45 domains (2, 4).”
• 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 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].”