<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Yoshino TP</submitter><funding>NIAID NIH HHS</funding><pagination>e1569</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3308936</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>6(3)</volume><pubmed_abstract>Recent evidence supports the involvement of inducible, highly diverse lectin-like recognition molecules in snail hemocyte-mediated responses to larval Schistosoma mansoni. Because host lectins likely are involved in initial parasite recognition, we sought to identify specific carbohydrate structures (glycans) shared between larval S. mansoni and its host Biomphalaria glabrata to address possible mechanisms of immune avoidance through mimicry of elements associated with the host immunoreactivity. A panel of monoclonal antibodies (mABs) to specific S. mansoni glycans was used to identify the distribution and abundance of shared glycan epitopes (glycotopes) on plasma glycoproteins from B. glabrata strains that differ in their susceptibilities to infection by S. mansoni. In addition, a major a</pubmed_abstract><journal>PLoS neglected tropical diseases</journal><pubmed_title>Glycotope sharing between snail hemolymph and larval schistosomes: larval transformation products alter shared glycan patterns of plasma proteins.</pubmed_title><pmcid>PMC3308936</pmcid><funding_grant_id>2R01AI015503</funding_grant_id><funding_grant_id>R01 AI015503</funding_grant_id><funding_grant_id>HHSN272201000005I</funding_grant_id><funding_grant_id>HHSN272201000005C</funding_grant_id><pubmed_authors>Liu H</pubmed_authors><pubmed_authors>Deelder AM</pubmed_authors><pubmed_authors>Hokke CH</pubmed_authors><pubmed_authors>Gonzalez LA</pubmed_authors><pubmed_authors>Wu XJ</pubmed_authors><pubmed_authors>Yoshino TP</pubmed_authors></additional><is_claimable>false</is_claimable><name>Glycotope sharing between snail hemolymph and larval schistosomes: larval transformation products alter shared glycan patterns of plasma proteins.</name><description>Recent evidence supports the involvement of inducible, highly diverse lectin-like recognition molecules in snail hemocyte-mediated responses to larval Schistosoma mansoni. Because host lectins likely are involved in initial parasite recognition, we sought to identify specific carbohydrate structures (glycans) shared between larval S. mansoni and its host Biomphalaria glabrata to address possible mechanisms of immune avoidance through mimicry of elements associated with the host immunoreactivity. A panel of monoclonal antibodies (mABs) to specific S. mansoni glycans was used to identify the distribution and abundance of shared glycan epitopes (glycotopes) on plasma glycoproteins from B. glabrata strains that differ in their susceptibilities to infection by S. mansoni. In addition, a major a</description><dates><release>2012-01-01T00:00:00Z</release><publication>2012</publication><modification>2025-04-05T11:10:38.198Z</modification><creation>2021-02-19T22:02:38Z</creation></dates><accession>S-EPMC3308936</accession><cross_references><pubmed>22448293</pubmed><doi>10.1371/journal.pntd.0001569</doi></cross_references></HashMap>