<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Crosnier C</submitter><funding>Medical Research Council</funding><funding>The Francis Crick Institute</funding><funding>Seventh Framework Programme</funding><funding>Royal Society</funding><funding>Wellcome Trust</funding><funding>Engineering and Physical Sciences Research Council</funding><pagination>14285-14299</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4933183</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>291(27)</volume><pubmed_abstract>Diversity at pathogen genetic loci can be driven by host adaptive immune selection pressure and may reveal proteins important for parasite biology. Population-based genome sequencing of Plasmodium falciparum, the parasite responsible for the most severe form of malaria, has highlighted two related polymorphic genes called dblmsp and dblmsp2, which encode Duffy binding-like (DBL) domain-containing proteins located on the merozoite surface but whose function remains unknown. Using recombinant proteins and transgenic parasites, we show that DBLMSP and DBLMSP2 directly and avidly bind human IgM via their DBL domains. We used whole genome sequence data from over 400 African and Asian P. falciparum isolates to show that dblmsp and dblmsp2 exhibit extreme protein polymorphism in their DBL domain,</pubmed_abstract><journal>The Journal of biological chemistry</journal><pubmed_title>Binding of Plasmodium falciparum Merozoite Surface Proteins DBLMSP and DBLMSP2 to Human Immunoglobulin M Is Conserved among Broadly Diverged Sequence Variants.</pubmed_title><pmcid>PMC4933183</pmcid><funding_grant_id>975281</funding_grant_id><funding_grant_id>MR/M006212/1</funding_grant_id><funding_grant_id>102541/A/13/Z</funding_grant_id><funding_grant_id>10097</funding_grant_id><funding_grant_id>242095</funding_grant_id><funding_grant_id>102541/Z/13/Z</funding_grant_id><funding_grant_id>098051</funding_grant_id><funding_grant_id>987447</funding_grant_id><funding_grant_id>MC_PC_12017</funding_grant_id><pubmed_authors>Rayner JC</pubmed_authors><pubmed_authors>Bustamante LY</pubmed_authors><pubmed_authors>Pleass RJ</pubmed_authors><pubmed_authors>Knuepfer E</pubmed_authors><pubmed_authors>Perrin AJ</pubmed_authors><pubmed_authors>Maciuca S</pubmed_authors><pubmed_authors>Miles A</pubmed_authors><pubmed_authors>Iqbal Z</pubmed_authors><pubmed_authors>Dougan G</pubmed_authors><pubmed_authors>Crosnier C</pubmed_authors><pubmed_authors>Goulding D</pubmed_authors><pubmed_authors>Wright GJ</pubmed_authors><pubmed_authors>Moore SC</pubmed_authors><pubmed_authors>Holder AA</pubmed_authors><pubmed_authors>Kamuyu G</pubmed_authors><pubmed_authors>Kwiatkowski DP</pubmed_authors></additional><is_claimable>false</is_claimable><name>Binding of Plasmodium falciparum Merozoite Surface Proteins DBLMSP and DBLMSP2 to Human Immunoglobulin M Is Conserved among Broadly Diverged Sequence Variants.</name><description>Diversity at pathogen genetic loci can be driven by host adaptive immune selection pressure and may reveal proteins important for parasite biology. Population-based genome sequencing of Plasmodium falciparum, the parasite responsible for the most severe form of malaria, has highlighted two related polymorphic genes called dblmsp and dblmsp2, which encode Duffy binding-like (DBL) domain-containing proteins located on the merozoite surface but whose function remains unknown. Using recombinant proteins and transgenic parasites, we show that DBLMSP and DBLMSP2 directly and avidly bind human IgM via their DBL domains. We used whole genome sequence data from over 400 African and Asian P. falciparum isolates to show that dblmsp and dblmsp2 exhibit extreme protein polymorphism in their DBL domain,</description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 Jul</publication><modification>2026-04-17T17:01:52.827Z</modification><creation>2019-03-27T02:17:36Z</creation></dates><accession>S-EPMC4933183</accession><cross_references><pubmed>27226583</pubmed><doi>10.1074/jbc.M116.722074</doi></cross_references></HashMap>