Evidence map›Paper›PMID 30367064›Full record

ArticleNature communications2018

Structural delineation of potent transmission-blocking epitope I on malaria antigen Pfs48/45.

Prasun Kundu, Anthony Semesi, Matthijs M Jore, Merribeth J Morin, Virginia L Price, Alice Liang, Jingxing Li, Kazutoyo Miura, Robert W Sauerwein, C Richter King and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.1field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

44 citing papers in PubMed, 76 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 6 institutions in 3 countries.

Prasun KunduProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, M5G 0A4, ON, Canada.
Anthony SemesiProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, M5G 0A4, ON, Canada.
Matthijs M JoreDepartment of Medical Microbiology, Radboud University Medical Center, Nijmegen, 6500 HB, Netherlands.
Merribeth J MorinPATH's Malaria Vaccine Initiative, Washington, 20001, DC, USA.
Virginia L PricePATH's Malaria Vaccine Initiative, Washington, 20001, DC, USA.
Alice LiangLakePharma Inc., Belmont, 94002, CA, USA.
Jingxing LiLakePharma Inc., Belmont, 94002, CA, USA.
Kazutoyo MiuraLaboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, 20852, MD, USA.
Robert W SauerweinDepartment of Medical Microbiology, Radboud University Medical Center, Nijmegen, 6500 HB, Netherlands.
C Richter KingPATH's Malaria Vaccine Initiative, Washington, 20001, DC, USA.
Jean-Philippe JulienProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, M5G 0A4, ON, Canada. jean-philippe.julien@sickkids.ca.ORCID http://orcid.org/0000-0001-7602-3995
U.S. President's Malaria Initiative · USHospital for Sick Children · CALakePharma (United States) · USRadboud University Nijmegen · NLNational Institutes of Health · USUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Interventions that can block the transmission of malaria-causing Plasmodium falciparum (Pf) between the human host and Anopheles vector have the potential to reduce the incidence of malaria. Pfs48/45 is a gametocyte surface protein critical for parasite development and transmission, and its targeting by monoclonal antibody (mAb) 85RF45.1 leads to the potent reduction of parasite transmission. Here, we reveal how the Pfs48/45 6C domain adopts a (SAG1)-related-sequence (SRS) fold. We structurally delineate potent epitope I and show how mAb 85RF45.1 recognizes an electronegative surface with nanomolar affinity. Analysis of Pfs48/45 sequences reveals that polymorphisms are rare for residues involved at the binding interface. Humanization of rat-derived mAb 85RF45.1 conserved the mode of recognition and activity of the parental antibody, while also improving its thermostability. Our work has implications for the development of transmission-blocking interventions, both through improving vaccine designs and the testing of passive delivery of mAbs in humans.

Indexed as

Amino Acid SequenceAnimalsAntibodies, MonoclonalAntibodies, Monoclonal, HumanizedAntibodies, ProtozoanAntigen-Antibody ReactionsAntigens, ProtozoanEpitopesHumansMalaria, FalciparumMalaria VaccinesMembrane GlycoproteinsModels, MolecularPlasmodium falciparumProtein DomainsProtein FoldingAntibodies, MonoclonalAntibodies, Monoclonal, HumanizedAntibodies, ProtozoanAntigens, ProtozoanEpitopesMalaria VaccinesMembrane Glycoproteinspfs48-45 protein, Plasmodium falciparumProtozoan Proteins

Identifiers

PMID30367064
PMCPMC6203815
OpenAlexW2896243600

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.