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J. Biol. Chem., Vol. 278, Issue 27, 24269-24276, July 4, 2003

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Porin OmpP2 of Haemophilus influenzae Shows Specificity for Nicotinamide-derived Nucleotide Substrates^*

Christian Andersen  , Elke Maier , Gabrielle Kemmer ¶, Julia Blass ¶, Anna-Karina Hilpert ¶, Roland Benz  || and Joachim Reidl ¶

From the Lehrstuhl für Biotechnologie, Biozentrum der Universität Würzburg, Am Hubland, D-97074 Würzburg, Germany and the ^¶Zentrum für Infektionsforschung, Universität Würzburg, Röntgenring 11, D-97070 Würzburg, Germany

Haemophilus influenzae has an absolute requirement for NAD (factor V) because it lacks all biosynthetic enzymes necessary for de novo synthesis of that cofactor. Therefore, growth in vitro requires the presence of NAD itself, NMN, or nicotinamide riboside (NR). To address uptake abilities of these compounds, we investigated outer membrane proteins. By analyzing ompP2 knockout mutants, we found that NAD and NMN uptake was prevented, whereas NR uptake was not. Through investigation of the properties of purified OmpP2 in artificial lipid membrane systems, the substrate specificity of OmpP2 for NAD and NMN was determined, with K_S values of 8 and 4mM, respectively, in 0.1 M KCl, whereas no interaction was detected for the nucleoside NR and other purine or pyrimidine nucleotide or nucleoside species. Based on our analysis, we assume that an intrinsic binding site within OmpP2 exists that facilitates diffusion of these compounds across the outer membrane, recognizing carbonyl and exposed phosphate groups. Because OmpP2 was formerly described as a general diffusion porin, an additional property of acting as a facilitator for nicotinamide-based nucleotide transport may have evolved to support and optimize utilization of the essential cofactor sources NAD and NMN in H. influenzae.

Received for publication, December 23, 2002 , and in revised form, April 8, 2003.

^* This work was supported in part by Deutsche Forschungsgemein-schaft Grants Be 865/10 and Re 1561/1 and the Fonds der Chemischen Industrie. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Recipient of an Emmy-Noether fellowship.

^|| To whom correspondence should be addressed. Tel.: 49-931-888-4501; Fax: 49-931-888-4509; E-mail: roland.benz{at}mail.uni-wuerzburg.de.

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