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J. Biol. Chem., Vol. 275, Issue 45, 34954-34962, November 10, 2000
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,
From the Division of Medical and Biochemical Microbiology, Research
Center Borstel, Center for Medicine and Biosciences, Parkallee
22, D-23845 Borstel, Germany
The lipopolysaccharide (LPS) of the deep rough
mutant Haemophilus influenzae I69 consists of lipid A and a
single 3-deoxy-D-manno-oct-2-ulosonic acid
(Kdo) residue substituted with one phosphate at position 4 or 5 (Helander, I. M., Lindner, B., Brade, H., Altmann, K., Lindberg, A. A., Rietschel, E. T., and Zähringer, U. (1988) Eur. J. Biochem. 177, 483-492). The
waaA gene encoding the essential LPS-specific Kdo
transferase was cloned from this strain, and its nucleotide sequence
was identical to H. influenzae DSM11121. The gene was
expressed in the Gram-positive host Corynebacterium glutamicum and characterized in vitro to encode a
monofunctional Kdo transferase. waaA of H. influenzae could not complement a knockout mutation in the
corresponding gene of an Re-type Escherichia coli strain.
However, complementation was possible by coexpressing the recombinant
waaA together with the LPS-specific Kdo kinase gene
(kdkA) of H. influenzae DSM11121 or I69,
respectively. The sequences of both kdkA genes were
determined and differed in 25 nucleotides, giving rise to six amino
acid exchanges between the deduced proteins. Both E. coli
strains which expressed waaA and kdkA from
H. influenzae synthesized an LPS containing a single Kdo
residue that was exclusively phosphorylated at position 4. The
structure was determined by nuclear magnetic resonance spectroscopy of
deacylated LPS. Therefore, the reaction products of both cloned Kdo
kinases represent only one of the two chemical structures synthesized
by H. influenzae I69.
The nucleotide sequences reported in this paper have been submitted to the DDBJ/GenBankTM/EBI Data Bank with accession numbers AJ277814, AJ277816, AJ277815, and AJ277817.
To whom correspondence should be addressed. Tel.: 49-4537188488;
Fax: 49-4537188686; E-mail:
wbrabetz@fz-borstel.de.
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