<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>78(9)</volume><submitter>Nampally M</submitter><pubmed_abstract>Chitin is the second most abundant polysaccharide, present, e.g., in insect and arthropod exoskeletons and fungal cell walls. In some species or under specific conditions, chitin appears to be enzymatically de-N-acetylated to chitosan-e.g., when pathogenic fungi invade their host tissues. Here, the deacetylation of chitin is assumed to represent a pathogenicity mechanism protecting the fungus from the host's chitin-driven immune response. While highly specific chitin binding lectins are well known and easily available, this is not the case for chitosan-specific probes. This is partly due to the poor antigenicity of chitosan so that producing high-affinity, specific antibodies is difficult. Also, lectins with specificity to chitosan have been described but are not commercially available, an</pubmed_abstract><journal>Applied and environmental microbiology</journal><pagination>3114-9</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3346462</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Fusion of a novel genetically engineered chitosan affinity protein and green fluorescent protein for specific detection of chitosan in vitro and in situ.</pubmed_title><pmcid>PMC3346462</pmcid><pubmed_authors>Kolkenbrock S</pubmed_authors><pubmed_authors>Nampally M</pubmed_authors><pubmed_authors>Moerschbacher BM</pubmed_authors></additional><is_claimable>false</is_claimable><name>Fusion of a novel genetically engineered chitosan affinity protein and green fluorescent protein for specific detection of chitosan in vitro and in situ.</name><description>Chitin is the second most abundant polysaccharide, present, e.g., in insect and arthropod exoskeletons and fungal cell walls. In some species or under specific conditions, chitin appears to be enzymatically de-N-acetylated to chitosan-e.g., when pathogenic fungi invade their host tissues. Here, the deacetylation of chitin is assumed to represent a pathogenicity mechanism protecting the fungus from the host's chitin-driven immune response. While highly specific chitin binding lectins are well known and easily available, this is not the case for chitosan-specific probes. This is partly due to the poor antigenicity of chitosan so that producing high-affinity, specific antibodies is difficult. Also, lectins with specificity to chitosan have been described but are not commercially available, an</description><dates><release>2012-01-01T00:00:00Z</release><publication>2012 May</publication><modification>2026-05-01T17:06:52.725Z</modification><creation>2019-03-27T00:53:12Z</creation></dates><accession>S-EPMC3346462</accession><cross_references><pubmed>22367086</pubmed><doi>10.1128/AEM.07506-11</doi><doi>10.1128/aem.07506-11</doi></cross_references></HashMap>