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Mutation in the Xanthomonas campestris xanA gene required for synthesis of xanthan and lipopolysaccharide drastically reduces the efficiency of bacteriophage (phi)L7 adsorption.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2002 Feb 22; Vol. 291 (2), pp. 338-43. - Publication Year :
- 2002
-
Abstract
- (Phi)L7 is a lytic phage infecting the gram-negative Xanthomonas campestis pv. campestris, a plant pathogen. To study phage-host interaction, a (phi)L7-resistant mutant was isolated from strain Xc17 by mini-Tn5 transposition and designated CH7LR. CH7LR could not plate (phi)L7 in double-layered assay and formed turbid clearing zones when the cell lawn was dropped with a high titer of (phi)L7. Sequence analysis showed that the mutated gene is xanA coding for phosphoglucomutase/phosphomannomutase, required for the synthesis of lipopolysaccharide and exopolysaccharide (xanthan). The involvement of xanA was confirmed by isolating another mutant with interrupted xanA and complementing with the cloned wild-type gene. Nonmucoid mutants are still sensitive to (phi)L7, indicating that xanthan is not involved in (phi)L7 adsorption. Since the mutants still exhibited low efficiencies of phage adsorption, we predict, by analogy with the cases in other bacteriophages of gram-negative bacteria, that other outer membrane components such as a protein are required for the formation of a complex receptor.<br /> (©2002 Elsevier Science (USA).)
- Subjects :
- Adsorption
Cloning, Molecular
Genes, Bacterial
Genetic Complementation Test
Host-Parasite Interactions
Mutagenesis, Insertional
Mutation
Phosphoglucomutase genetics
Phosphoglucomutase physiology
Phosphotransferases (Phosphomutases) genetics
Phosphotransferases (Phosphomutases) physiology
Transposases genetics
Transposases physiology
Virus Integration
Xanthomonas campestris enzymology
Bacteriophages physiology
Lipopolysaccharides biosynthesis
Polysaccharides, Bacterial biosynthesis
Xanthomonas campestris metabolism
Xanthomonas campestris virology
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 291
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 11846409
- Full Text :
- https://doi.org/10.1006/bbrc.2002.6440