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Originally published as Biophys J. BioFAST on October 20, 2006.
doi:10.1529/biophysj.106.095273
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Biophysical Journal 92:588-593 (2007)
© 2007 The Biophysical Society

Haemophilus influenzae Outer Membrane Protein P5 Is Associated with Inorganic Polyphosphate and Polyhydroxybutyrate

E. Zakharian and R. N. Reusch

Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, Michigan

Correspondence: Address reprint requests to Rosetta N. Reusch, Tel.: 517-355-6463; Fax: 517-353-8957; E-mail: rnreusch{at}msu.edu.

Outer membrane protein P5 of nontypeable (acapsulate) Haemophilus influenzae (NTHi P5) forms large pores in planar lipid bilayers between symmetric solutions that unpredictably display a nonzero reversal potential. Moreover, NTHi P5 has a high theoretical isoelectric point, calculated as 9.58, which is not in agreement with the experimental isoelectric point, determined as 6.3–6.8, or with its preference for cations, disproportionately strong at one side. These anomalous results intimate that NTHi P5 is associated with a polyanion. Chemical and immunological analyses revealed the presence of inorganic polyphosphate (polyP), and the amphiphilic, solvating polyester, poly-(R)-3-hydroxybutyrate, frequently associated with polyP. A sharp reduction in cation selectivity was observed after addition of Saccharomyces cerevisiae exopolyphosphatase X to the bilayer, providing functional evidence for the involvement of polyP in selectivity. The results suggest that NTHi P5 associates with polyP and poly-(R)-3-hydroxybutyrate to create large, cation-selective pores in the outer membrane of H. influenzae.




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R. O. Blaustein
On the Impossibility of Nonzero Reversal Potentials of Passive Pores Separating Symmetric Solutions: Comment on Haemophilus influenzae Outer Membrane Protein P5 Is Associated with Inorganic Polyphosphate and Polyhydroxybutyrate
Biophys. J., October 15, 2007; 93(8): 2978 - 2978.
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