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    <!-- http://purl.obolibrary.org/obo/IDO_0100827 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/IDO_0100827">
        <rdfs:label>B.suis virB9 mutant</rdfs:label>
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    <!-- http://purl.obolibrary.org/obo/IDO_0100879 -->

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        <rdfs:label xml:lang="en">attenuated disposition</rdfs:label>
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    <!-- http://purl.obolibrary.org/obo/IDO_0110291 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/IDO_0110291">
        <rdfs:label>B. melitensis 16M virb9 mutant</rdfs:label>
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        <ns3:IAO_0000115>A mutant of strain Brucella melitensis bv. 1 str. 16M that lacks an intact gene virb9.</ns3:IAO_0000115>
        <ns3:IAO_0000119>PMID: 11349069, 10510235, 11437834, 12414149</ns3:IAO_0000119>
        <ns3:IAO_0000117>YH</ns3:IAO_0000117>
        <rdfs:seeAlso>NCBIGene: 1197804</rdfs:seeAlso>
        <rdfs:comment>The gene virb9 from the strain Brucella melitensis bv. 1 str. 16M is a virulence gene.</rdfs:comment>
        <rdfs:comment>Information about the mutated molecule: MUTATION: Uptake in the presence or absence of Ca2 and Mg2 did not influence the subsequent intracellular survival of wild-type Brucella, whereas the decrease in the number of surviving  virB9 mutant  cells was delayed in the absence of Ca2 and Mg2. Possibly two types of adhesion molecules promoted uptake of Brucella, one being Ca2 and Mg2 dependent and the other not, and that both types participate in the uptake of wild-type bacteria but only the latter type participates in the uptake of the  virB9   mutant [Ref6545:Rittig et al., 2001].   Four independent  mutants in virB5, virB9 or virB10 were highly attenuated in an in vitro infection model with human macrophages [Ref6467:O&#39;Callaghan et al., 1999].  The intracellular fate of three virB  mutants (virB2, virB4 and  virB9) in HeLa cells by immunofluorescence was examined. The three VirB proteins are not necessary for penetration and the inhibition of phago-lysosomal fusion within non-professional phagocytes. Rather, the virB mutants  are unable to reach the replicative niche and reside in a membrane -bound vacuole expressing the late endosomal marker, LAMP1, and the sec61beta protein from the ER membrane, proteins that are present in autophagic vesicles originating from the ER [Ref6546:Delrue et al., 2001].  Attenuated non-polar virB2, virB4, virB8, virB9 and virB10 Brucella  mutants are capable of penetrating cells as the same rate as the virulent wild-type Brucella, transit through EEA1 -positive early compartments and then localize in LAMP1-positive compartments at early times of infection [Ref6466:Gorvel and Moreno, 2002].</rdfs:comment>
        <rdfs:seeAlso>UniProtKB accession: Q8YDZ1</rdfs:seeAlso>
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        <rdfs:label>CHANNEL PROTEIN VIRB9 HOMOLOG</rdfs:label>
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