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The Sv40 Late Protein Vp4 Is A Viroporin That Forms Pores To Disrupt Membranes For Viral Release, Smita Raghava, Kristen M. Giorda, F. B. Romano, Alejandro P. Heuck, Daniel Hebert
The Sv40 Late Protein Vp4 Is A Viroporin That Forms Pores To Disrupt Membranes For Viral Release, Smita Raghava, Kristen M. Giorda, F. B. Romano, Alejandro P. Heuck, Daniel Hebert
Alejandro P. Heuck
Nonenveloped viruses are generally released by the timely lysis of the host cell by a poorly understood process. For the nonenveloped virus SV40, virions assemble in the nucleus and then must be released from the host cell without being encapsulated by cellular membranes. This process appears to involve the well-controlled insertion of viral proteins into host cellular membranes rendering them permeable to large molecules. VP4 is a newly identified SV40 gene product that is expressed at late times during the viral life cycle that corresponds to the time of cell lysis. To investigate the role of this late expressed protein …
The Transition From Closed To Open Conformation Of Treponema Pallidum Outer Membrane-Associated Lipoprotein Tp0453 Involves Membrane Sensing And Integration By Two Amphipathic Helices, Amit Luthra, Guangyu Zhu, Daniel C. Desrosiers, Christian H. Eggers, Vishwaroop Mulay, Arvind Anand, Fiona A. Mcarthur, Fabian B. Romano, Melissa J. Caimano, Alejandro P. Heuck, Michael G. Malkowski, Justin D. Radolf
The Transition From Closed To Open Conformation Of Treponema Pallidum Outer Membrane-Associated Lipoprotein Tp0453 Involves Membrane Sensing And Integration By Two Amphipathic Helices, Amit Luthra, Guangyu Zhu, Daniel C. Desrosiers, Christian H. Eggers, Vishwaroop Mulay, Arvind Anand, Fiona A. Mcarthur, Fabian B. Romano, Melissa J. Caimano, Alejandro P. Heuck, Michael G. Malkowski, Justin D. Radolf
Alejandro P. Heuck
The molecular architecture and composition of the outer membrane (OM) of Treponema pallidum (Tp), the noncultivable agent of venereal syphilis, differ considerably from those of typical Gram-negative bacteria. Several years ago we described TP0453, the only lipoprotein associated with the inner leaflet of the Tp OM. Whereas polypeptides of other treponemal lipoproteins are hydrophilic, non-lipidated TP0453 can integrate into membranes, a property attributed to its multiple amphipathic helices (AHs). Furthermore, membrane integration of the TP0453 polypeptide was found to increase membrane permeability, suggesting the molecule functions in a porin-like manner. To better understand the mechanism of membrane integration of TP0453 …
Efficient Isolation Of Pseudomonas Aeruginosa Type Iii Secretion Translocators And Assembly Of Heteromeric Transmembrane Pores In Model Membranes, Fabian B. Romano, Kyle C. Rossi, Christos G. Sava, Andreas Holzenburg, Eugenia M. Clerico, Alejandro P. Heuck
Efficient Isolation Of Pseudomonas Aeruginosa Type Iii Secretion Translocators And Assembly Of Heteromeric Transmembrane Pores In Model Membranes, Fabian B. Romano, Kyle C. Rossi, Christos G. Sava, Andreas Holzenburg, Eugenia M. Clerico, Alejandro P. Heuck
Alejandro P. Heuck
Translocation of bacterial toxins or effectors into host cells using the type III secretion (T3S) system is a conserved mechanism shared by many Gram-negative pathogens. Pseudomonas aeruginosa injects different proteins across the plasma membrane of target cells, altering the normal metabolism of the host. Protein translocation presumably occurs through a proteinaceous transmembrane pore formed by two T3S secreted protein translocators, PopB and PopD. Unfolded translocators are secreted through the T3S needle prior to insertion into the target membrane. Purified PopB and PopD form pores in model membranes. However, their tendency to form heterogeneous aggregates in solution had hampered the analysis …