<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-06-01T04:36:04Z</responseDate><request verb="GetRecord" identifier="oai:riuma.uma.es:10630/37375" metadataPrefix="qdc">https://riuma.uma.es/rest/oai/request</request><GetRecord><record><header><identifier>oai:riuma.uma.es:10630/37375</identifier><datestamp>2026-02-03T11:08:34Z</datestamp><setSpec>com_10630_2254</setSpec><setSpec>col_10630_37953</setSpec></header><metadata><qdc:qualifieddc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:doc="http://www.lyncode.com/xoai" xmlns:qdc="http://dspace.org/qualifieddc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://purl.org/dc/elements/1.1/ http://dublincore.org/schemas/xmls/qdc/2006/01/06/dc.xsd http://purl.org/dc/terms/ http://dublincore.org/schemas/xmls/qdc/2006/01/06/dcterms.xsd http://dspace.org/qualifieddc/ http://www.ukoln.ac.uk/metadata/dcmi/xmlschema/qualifieddc.xsd">
   <dc:title>PipB2 is a substrate of the Salmonella pathogenicity island 1- encoded type III secretion system</dc:title>
   <dc:creator>Baisón-Olmo, Fernando</dc:creator>
   <dc:creator>Cardenal Muñoz, Elena</dc:creator>
   <dc:creator>Ramos Morales, Francisco</dc:creator>
   <dc:subject>Salmonella</dc:subject>
   <dcterms:abstract>Salmonella harbors two type III secretion systems, T3SS1 and T3SS2, encoded on the&#xd;
pathogenicity islands SPI1 and SPI2, respectively. Several effector proteins are secreted&#xd;
through these systems into the eukaryotic host cells. PipB2 is a T3SS2 effector that&#xd;
contributes to the modulation of kinesin-1 motor complex activity. Here, we show that&#xd;
PipB2 is also a substrate of T3SS1. This result was obtained infecting human epithelial&#xd;
HeLa cells for 2 hours and was confirmed in murine RAW264.7 macrophages, and rat&#xd;
NRK fibroblasts. Analysis at different time points after infection revealed that&#xd;
translocation of PipB2 is T3SS1-dependent in epithelial cells throughout the infection.&#xd;
In contrast, translocation into macrophages is T3SS1-dependent during invasion but&#xd;
T3SS2-dependent at later time points. The N-terminal 10 amino acid residues contain&#xd;
the signal necessary for translocation through both systems. These results confirm the&#xd;
functional overlap between these virulence-related secretion systems and suggest a new&#xd;
role for the effector PipB2</dcterms:abstract>
   <dcterms:dateAccepted>2025-01-30T10:21:40Z</dcterms:dateAccepted>
   <dcterms:available>2025-01-30T10:21:40Z</dcterms:available>
   <dcterms:created>2025-01-30T10:21:40Z</dcterms:created>
   <dcterms:issued>2012-06-29</dcterms:issued>
   <dc:type>journal article</dc:type>
   <dc:identifier>Baisón-Olmo F, Cardenal-Muñoz E, Ramos-Morales F. PipB2 is a substrate of the Salmonella pathogenicity island 1-encoded type III secretion system. Biochem Biophys Res Commun. 2012 Jun 29;423(2):240-6. doi: 10.1016/j.bbrc.2012.05.095. Epub 2012 May 26. PMID: 22640733.</dc:identifier>
   <dc:identifier>https://hdl.handle.net/10630/37375</dc:identifier>
   <dc:identifier>10.1016/j.bbrc.2012.05.095</dc:identifier>
   <dc:language>eng</dc:language>
   <dc:rights>open access</dc:rights>
   <dc:publisher>Elvervier</dc:publisher>
</qdc:qualifieddc>
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