<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>Burri DJ</dc:creator>
  <dc:creator>da Palma JR</dc:creator>
  <dc:creator>Seidah NG</dc:creator>
  <dc:creator>Zanotti G</dc:creator>
  <dc:creator>Cendron L</dc:creator>
  <dc:creator>Pasquato A</dc:creator>
  <dc:creator>Kunz S</dc:creator>
  <dc:date>2013</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">The arenaviruses are an important family of emerging viruses that includes several causative agents of severe hemorrhagic fevers in humans that represent serious public health problems. A crucial step of the arenavirus life cycle is maturation of the envelope glycoprotein precursor (GPC) by the cellular subtilisin kexin isozyme 1 (SKI-1)/site 1 protease (S1P). Comparison of the currently known sequences of arenavirus GPCs revealed the presence of a highly conserved aromatic residue at position P7 relative to the SKI-1/S1P cleavage side in Old World and clade C New World arenaviruses but not in New World viruses of clades A and B or cellular substrates of SKI-1/S1P. Using a combination of molecular modeling and structure-function analysis, we found that residue Y285 of SKI-1/S1P, distal from the catalytic triad, is implicated in the molecular recognition of the aromatic "signature residue" at P7 in the GPC of Old World Lassa virus. Using a quantitative biochemical approach, we show that Y285 of SKI-1/S1P is crucial for the efficient processing of peptides derived from Old World and clade C New World arenavirus GPCs but not of those from clade A and B New World arenavirus GPCs. The data suggest that during coevolution with their mammalian hosts, GPCs of Old World and clade C New World viruses expanded the molecular contacts with SKI-1/S1P beyond the classical four-amino-acid recognition sequences and currently occupy an extended binding pocket.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://sonar.ch/global/documents/122965</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1128/JVI.00072-13</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/pmid/23536681</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:source>Journal of virology. - 2013</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">Amino Acid Motifs</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">Amino Acid Sequence</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">Animals</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">Arenaviridae Infections</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">Arenaviruses, New World</dc:subject>
  <dc:subject xmlns:ns6="xml" ns6:lang="en">Arenaviruses, Old World</dc:subject>
  <dc:subject xmlns:ns7="xml" ns7:lang="en">CHO Cells</dc:subject>
  <dc:subject xmlns:ns8="xml" ns8:lang="en">Cricetinae</dc:subject>
  <dc:subject xmlns:ns9="xml" ns9:lang="en">Humans</dc:subject>
  <dc:subject xmlns:ns10="xml" ns10:lang="en">Molecular Sequence Data</dc:subject>
  <dc:subject xmlns:ns11="xml" ns11:lang="en">Proprotein Convertases</dc:subject>
  <dc:subject xmlns:ns12="xml" ns12:lang="en">Protein Processing, Post-Translational</dc:subject>
  <dc:subject xmlns:ns13="xml" ns13:lang="en">Sequence Alignment</dc:subject>
  <dc:subject xmlns:ns14="xml" ns14:lang="en">Serine Endopeptidases</dc:subject>
  <dc:subject xmlns:ns15="xml" ns15:lang="en">Viral Envelope Proteins</dc:subject>
  <dc:title xmlns:ns16="xml" ns16:lang="en">Differential recognition of Old World and New World arenavirus envelope glycoproteins by subtilisin kexin isozyme 1 (SKI-1)/site 1 protease (S1P).</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>