<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Wang Z</submitter><funding>NIAID NIH HHS</funding><pagination>606-16</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3028840</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>79(2)</volume><pubmed_abstract>During group B streptococcal infection, the alpha C protein (ACP) on the bacterial surface binds to host cell surface heparan sulfate proteoglycans (HSPGs) and facilitates entry of bacteria into human epithelial cells. Previous studies in a Drosophila melanogaster model showed that binding of ACP to the sulfated polysaccharide chains (glycosaminoglycans) of HSPGs promotes host death and is associated with higher bacterial burdens. We hypothesized that ACP-glycosaminoglycan binding might determine infection outcome by altering host responses to infection, such as expression of antimicrobial peptides. As glycosaminoglycans/HSPGs also interact with a number of endogenous secreted signaling molecules in Drosophila, we examined the effects of host and pathogen glycosaminoglycan/HSPG-binding str</pubmed_abstract><journal>Infection and immunity</journal><pubmed_title>Host and pathogen glycosaminoglycan-binding proteins modulate antimicrobial peptide responses in Drosophila melanogaster.</pubmed_title><pmcid>PMC3028840</pmcid><funding_grant_id>AI059495</funding_grant_id><funding_grant_id>U54 AI057159</funding_grant_id><funding_grant_id>AI057159</funding_grant_id><funding_grant_id>K08 AI059495</funding_grant_id><pubmed_authors>Linhardt RJ</pubmed_authors><pubmed_authors>Kemp MM</pubmed_authors><pubmed_authors>Flax LA</pubmed_authors><pubmed_authors>Baron MJ</pubmed_authors><pubmed_authors>Wang Z</pubmed_authors></additional><is_claimable>false</is_claimable><name>Host and pathogen glycosaminoglycan-binding proteins modulate antimicrobial peptide responses in Drosophila melanogaster.</name><description>During group B streptococcal infection, the alpha C protein (ACP) on the bacterial surface binds to host cell surface heparan sulfate proteoglycans (HSPGs) and facilitates entry of bacteria into human epithelial cells. Previous studies in a Drosophila melanogaster model showed that binding of ACP to the sulfated polysaccharide chains (glycosaminoglycans) of HSPGs promotes host death and is associated with higher bacterial burdens. We hypothesized that ACP-glycosaminoglycan binding might determine infection outcome by altering host responses to infection, such as expression of antimicrobial peptides. As glycosaminoglycans/HSPGs also interact with a number of endogenous secreted signaling molecules in Drosophila, we examined the effects of host and pathogen glycosaminoglycan/HSPG-binding str</description><dates><release>2011-01-01T00:00:00Z</release><publication>2011 Feb</publication><modification>2025-04-05T00:26:53.166Z</modification><creation>2019-03-27T00:38:27Z</creation></dates><accession>S-EPMC3028840</accession><cross_references><pubmed>21078848</pubmed><doi>10.1128/iai.00254-10</doi><doi>10.1128/IAI.00254-10</doi></cross_references></HashMap>