<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">McNamara, Michael</style></author><author><style face="normal" font="default" size="100%">Danelishvili, Lia</style></author><author><style face="normal" font="default" size="100%">Bermudez, Luiz E</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The Mycobacterium avium ESX-5 PPE protein, PPE25-MAV, interacts with an ESAT-6 family Protein, MAV_2921, and localizes to the bacterial surface.</style></title><secondary-title><style face="normal" font="default" size="100%">Microbial pathogenesis</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Microb. Pathog.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid Motifs</style></keyword><keyword><style  face="normal" font="default" size="100%">Bacterial Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Membrane</style></keyword><keyword><style  face="normal" font="default" size="100%">Mycobacterium avium</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Binding</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Transport</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2012</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2012 Apr</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">52</style></volume><pages><style face="normal" font="default" size="100%">227-38</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Previous research has demonstrated that inactivation of the Mycobacterium avium gene, PPE25-MAV (MAV_2928), leads to a significant attenuation of virulence in both in vitro and in vivo models. PPE25-MAV encodes for a PPE family protein, a family from which many members have been implicated in both bacterial virulence and host immune recognition. Recent research has shown that many PPE family proteins are exported by a specialized Type VII secretion system in mycobacteria. In this context, the mechanisms of PPE25-MAV in M. avium pathogenesis were investigated. A mycobacterial 2-hybrid system was used to perform a directed search for M. avium proteins that interact directly with PPE25-MAV. An interaction was observed between PPE25-MAV and the ESAT-6 family protein, MAV_2921, and was further defined by 2-hybrid analysis of truncated PPE25-MAV, and confirmed by co-immunoprecipitation. Localization of the PPE25-MAV protein was analyzed in Mycobacterium smegmatis expressing the recombinant protein and a significant percentage of PPE25-MAV was shown to be exposed at the bacterial surface by surface biotinylation and trypsin protection assays. Finally, transcriptional analysis of PPE25-MAV and its associated operon suggested that nutrient limitation, a condition which occurs in the phagosome, plays a role in regulating expression of the PPE25-MAV gene.</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/22265661?dopt=Abstract</style></custom1></record></records></xml>