scholarly journals Virulence-associated chromosome locus J, VacJ, an outer membrane lipoprotein elicits protective immunity against Acinetobacter baumannii infection in mice

2020 ◽  
Vol 20 (4) ◽  
Author(s):  
Saeideh Masoumkhani ◽  
Shakiba Darvish Alipour Astaneh ◽  
Abolfazl Jahangiri ◽  
Iraj Rasooli
Keyword(s):  
Acinetobacter Baumannii ◽  
Outer Membrane ◽  
Protective Immunity ◽  
Outer Membrane Lipoprotein ◽  
Membrane Lipoprotein

Backbone resonance assignments of the outer membrane lipoprotein FrpD from Neisseria meningitidis

2012 ◽  
Vol 8 (1) ◽  
pp. 53-55 ◽  
Author(s):  
Ladislav Bumba ◽  
Ekaterina Sviridova ◽  
Ivana Kutá Smatanová ◽  
Pavlína Řezáčová ◽  
Václav Veverka
Keyword(s):  
Neisseria Meningitidis ◽  
Outer Membrane ◽  
Resonance Assignments ◽  
Backbone Resonance Assignments ◽  
Backbone Resonance ◽  
Outer Membrane Lipoprotein ◽  
Membrane Lipoprotein

scholarly journals Role of the Pilot Protein YscW in the Biogenesis of the YscC Secretin in Yersinia enterocolitica

2004 ◽  
Vol 186 (16) ◽  
pp. 5366-5375 ◽  
Author(s):  
Peter Burghout ◽  
Frank Beckers ◽  
Emmie de Wit ◽  
Ria van Boxtel ◽  
Guy R. Cornelis ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Yersinia Enterocolitica ◽  
Amino Acid Residues ◽  
Wild Type ◽  
C Terminus ◽  
Outer Membrane Lipoprotein ◽  
Protein Secretion System ◽  
Membrane Lipoprotein ◽  
Type Iii Protein Secretion

ABSTRACT The YscC secretin is a major component of the type III protein secretion system of Yersinia enterocolitica and forms an oligomeric structure in the outer membrane. In a mutant lacking the outer membrane lipoprotein YscW, secretion is strongly reduced, and it has been proposed that YscW plays a role in the biogenesis of the secretin. To study the interaction between the secretin and this putative pilot protein, YscC and YscW were produced in trans in a Y. enterocolitica strain lacking all other components of the secretion machinery. YscW expression increased the yield of oligomeric YscC and was required for its outer membrane localization, confirming the function of YscW as a pilot protein. Whereas the pilot-binding site of other members of the secretin family has been identified in the C terminus, a truncated YscC derivative lacking the C-terminal 96 amino acid residues was functional and stabilized by YscW. Pulse-chase experiments revealed that ∼30 min were required before YscC oligomerization was completed. In the absence of YscW, oligomerization was delayed and the yield of YscC oligomers was strongly reduced. An unlipidated form of the YscW protein was not functional, although it still interacted with the secretin and caused mislocalization of YscC even in the presence of wild-type YscW. Hence, YscW interacts with the unassembled YscC protein and facilitates efficient oligomerization, likely at the outer membrane.

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