Identification and imaging of peptides and proteins on Enterococcus faecalis biofilms by matrix assisted laser desportion ionization mass spectrometry

dc.contributor.authorBlaze, M. T.
dc.contributor.authorAydin, B.
dc.contributor.authorCarlson, Ross P.
dc.contributor.authorHanley, L.
dc.date.accessioned2017-01-31T20:56:50Z
dc.date.available2017-01-31T20:56:50Z
dc.date.issued2012-09
dc.description.abstractThe heptapeptide ARHPHPH was identified from biofilms and planktonic cultures of two different strains of Enterococcus faecalis, V583 and ATCC 29212, using matrix assisted laser desorption ionization mass spectrometry (MALDI-MS). ARHPHPH was also imaged at the boundary of cocultured, adjacent E. faecalis and Escherichia coli (ATCC 25922) biofilms, appearing only on the E. faecalis side. ARHPHPH was proteolyzed from κ-casein, a component in the growth media, by E. faecalis microbes. Additionally, top down and bottom up proteomic approaches were combined to identify and spatially locate multiple proteins within intact E. faecalis V583 biofilms by MALDI-MS. The resultant tandem MS data were searched against the NCBInr E. faecalis V583 database to identify thirteen cytosolic and membrane proteins which have functional association with the cell surface. Two of these proteins, enolase and GAPDH, are glycolytic enzymes known to display multiple functions in bacterial virulence in related bacterial strains. This work illustrates a powerful approach for discovering and localizing multiple peptides and proteins within intact biofilms.en_US
dc.identifier.citationBlaze MT, Aydin B, Carlson RP, Hanley L , "Identification and imaging of peptides and proteins on Enterococcus faecalis biofilms by matrix assisted laser desportion ionization mass spectrometry," Analyst, September 2012 137(21): 5018-5025.en_US
dc.identifier.issn0003-2654
dc.identifier.urihttps://scholarworks.montana.edu/handle/1/12492
dc.titleIdentification and imaging of peptides and proteins on Enterococcus faecalis biofilms by matrix assisted laser desportion ionization mass spectrometryen_US
dc.typeArticleen_US
mus.citation.extentfirstpage5018en_US
mus.citation.extentlastpage5025en_US
mus.citation.issue21en_US
mus.citation.journaltitleAnalysten_US
mus.citation.volume137en_US
mus.data.thumbpage7en_US
mus.identifier.categoryChemical & Material Sciencesen_US
mus.identifier.categoryEngineering & Computer Scienceen_US
mus.identifier.categoryHealth & Medical Sciencesen_US
mus.identifier.categoryPhysics & Mathematicsen_US
mus.identifier.doi10.1039/c2an35922gen_US
mus.relation.collegeCollege of Agricultureen_US
mus.relation.collegeCollege of Engineeringen_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.departmentCell Biology & Neuroscience.en_US
mus.relation.departmentCenter for Biofilm Engineering.en_US
mus.relation.departmentChemical & Biological Engineering.en_US
mus.relation.departmentChemical Engineering.en_US
mus.relation.departmentChemistry & Biochemistry.en_US
mus.relation.departmentMicrobiology & Immunology.en_US
mus.relation.researchgroupCenter for Biofilm Engineering.en_US
mus.relation.universityMontana State University - Bozemanen_US

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