<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Schneiter, Roger</dc:creator>
  <dc:creator>Pietro, Antonio Di</dc:creator>
  <dc:date>2013-10-01</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">CAP superfamily proteins, also known as sperm-coating proteins, are found in all  kingdoms of life and have been implicated in a variety of physiological contexts,  including immune defense in plants and mammals, sperm maturation and fertilization,  fungal virulence, and toxicity of insect and reptile venoms as well as prostate and  brain cancer. CAP family members are mostly secreted glycoproteins that are highly  stable in the extracellular fluid. All members of the superfamily share a common CAP  domain of approximately 150 amino acids, which adopts a unique α-β-α sandwich  fold. The conserved structure suggests that CAP proteins exert fundamentally similar  functions. However, the molecular mode of action of this protein family has remained  enigmatic. The budding yeast Saccharomyces cerevisiae has three CAP family  members designated Pry (pathogen related in yeast), and recent evidence indicates  that they act as sterol-binding and export proteins. Expression of the mammalian CAP  protein CRISP2, which binds sterols in vitro, complements the sterol export defect of a  yeast pry mutant, suggesting that sterol binding and export is conserved among  different CAP family members. Collectively, these observations suggest that CAP  family members constitute a novel class of secreted extracellular sterol-binding  proteins. A ligand-binding activity of the CAP domain could explain many of the  biological activities attributed to these proteins. For example, the strong induction of  plant pathogenesis-related 1 protein upon exposure to pathogens may serve to inhibit  pathogen proliferation by extracting sterols from the pathogen membrane. Similarly,  the presence of these proteins in the venom of toxic insects and reptiles or in the  secretome of pathogenic fungi might inflict damage by sequestering sterols or related  small hydrophobic compounds from the host tissue.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://folia.unifr.ch/global/documents/303256</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/303256/files/bmc-2013-0021.pdf</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1515/bmc-2013-0021</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>License undefined</dc:rights>
  <dc:source>BioMolecular Concepts. - 2013, vol. 4, no. 5, p. 519-525</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">fungal virulence</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">Fusarium oxysporum</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">mouse infection model</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">pathogenesis related PR 1</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">sterol detoxification</dc:subject>
  <dc:subject>info:eu-repo/classification/udc/57</dc:subject>
  <dc:title xmlns:ns6="xml" ns6:lang="en">The CAP protein superfamily: function in sterol export and fungal virulence</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
