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Antimicrobial Agents and Chemotherapy, February 1999, p. 226-232, Vol. 43, No. 2
0066-4804/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Variation in the Composition and Pore Function of Major Outer Membrane Pore Protein P2 of Haemophilus influenzae from Cystic Fibrosis Patients

Annette G. Regelink,1 David Dahan,2 Lieke V. M. Möller,1,3 James W. Coulton,2 Paul Eijk,1 Peter Van Ulsen,1 Jacob Dankert,1 and Loek Van Alphen1,*

Department of Medical Microbiology, University of Amsterdam, Academic Medical Center, Amsterdam,1 and Department of Medical Microbiology, University Hospital Groningen, and Laboratory of Public Health Groningen, Groningen,3 The Netherlands, and Department of Microbiology and Immunology, McGill University, Montréal, Québec, Canada H3A 2B42

Received 22 April 1998/Returned for modification 18 August 1998/Accepted 2 November 1998

We investigated the relationship between susceptibility to beta -lactam antibiotics and variation in the major outer membrane protein P2 (OmpP2; also called porin) of persistent nonencapsulated Haemophilus influenzae isolated from cystic fibrosis patients. Nine OmpP2 variants were selected from two distinct H. influenzae strains from two patients extensively treated with beta -lactam antibiotics. The variants differed in their susceptibilities to at least two beta -lactam antibiotics. By detergent extraction and column chromatography, OmpP2 was purified from two variants that were derived from strain 70 and that differed notably in their susceptibilities to beta -lactam antibiotics. The proteins were reconstituted into black lipid membranes for measurement of porin function. OmpP2 from the more resistant isolate (isolate 70b) had a smaller channel conductance than OmpP2 of the more susceptible isolate (isolate 70f). DNA sequencing of ompP2 of these isolates revealed single nonsynonymous base differences; there were changes in the amino acid sequence corresponding to surface-exposed loops 4, 5, 6, and 8. Changes in loops 4, 5, and 6 were previously shown to result in antigenic differences. Beside these mutations, variants of strain 70 showed additional mutations in loop 1 and nonexposed loop 3. Taken together, our results suggest that in variants of strain 70, nonsynonymous point mutations accumulated both in the sequences of ompP2 coding for antigen-variable loops and in other loops, notably, loops 1 and 3. The latter changes are suggested to affect the permeability of the porin channel.

* Corresponding author. Mailing address: Laboratory for Vaccine Research (LVR), P.O. Box 1, NL-3720 BA Bilthoven, The Netherlands. Phone: 31-20-2742701. Fax: 31-30-2744429. E-mail: Loek.van.Alphen{at}rivm.nl.

Antimicrobial Agents and Chemotherapy, February 1999, p. 226-232, Vol. 43, No. 2
0066-4804/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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