Simple jQuery Dropdowns
Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/33486
Full metadata record
DC FieldValueLanguage
dc.contributor.authorAttasit Udompetcharapornen_US
dc.contributor.authorKingkamon Junkunloen_US
dc.contributor.authorSaengchan Senapinen_US
dc.contributor.authorSittiruk Roytrakulen_US
dc.contributor.authorTimothy W. Flegelen_US
dc.contributor.authorKallaya Sritunyalucksanaen_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherEvolutionary Biology Centreen_US
dc.contributor.otherThailand National Center for Genetic Engineering and Biotechnologyen_US
dc.date.accessioned2018-11-09T02:00:18Z-
dc.date.available2018-11-09T02:00:18Z-
dc.date.issued2014-01-01en_US
dc.identifier.citationDevelopmental and Comparative Immunology. Vol.46, No.2 (2014), 146-154en_US
dc.identifier.issn18790089en_US
dc.identifier.issn0145305Xen_US
dc.identifier.other2-s2.0-84900553144en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84900553144&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/33486-
dc.description.abstractIn an attempt to identify a peptidoglycan recognition protein (PGRP) in Penaeus (Penaeus) monodon, in vitro pull-down binding assays were used between shrimp proteins and purified peptidoglycan (PG). By gel electrophoresis and mass spectrometry followed by Mascot program analysis, proteins from shrimp hemocyte peripheral membrane proteins showed significant homology to records for a QM protein, actin and prophenoloxidase 2 precursor (proPO2), while proteins from cell-free plasma showed significant homology to records for a vitellogenin, a fibrinogen related protein (FREP) and a C-type lectin. Due to time and resource limitations, specific binding to PG was examined only for recombinant PmQM protein and PmLec that were synthesized based on sequences reported in the Genbank database (accession numbers FJ766846 and DQ078266, respectively). An in vitro assay revealed that hemocytes would bind with and encapsulate agarose beads coated with recombinant PmQM (rPmQM) or rPmLec and that melanization followed 2. h post-encapsulation. ELISA tests confirmed specific binding of rPmQM protein to PG. This is the first time that PmQM has been reported as a potential PGRP in shrimp or any other crustacean. The two other potential PGRP identified (FREP and the vitellin-like protein present in male P. monodon, unlike other vitellin subunits) should also be expressed heterologously and tested for their ability to activate shrimp hemocytes. © 2014 Elsevier Ltd.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84900553144&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectImmunology and Microbiologyen_US
dc.titleIdentification and characterization of a QM protein as a possible peptidoglycan recognition protein (PGRP) from the giant tiger shrimp Penaeus monodonen_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1016/j.dci.2014.04.003en_US
Appears in Collections:Scopus 2011-2015

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.