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Gene Review:

lytB - endo-beta-N-acetylglucosaminidase

Streptococcus pneumoniae R6

Muramatsu, H. et al., Martín-Galiano, A.J. et al., Mizuochi, T. et al., Moscoso, M. et al., De Las Rivas, B. et al., et al.

Martín-Galiano, Wells, de la Campa,

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Disease relevance of lytB

To determine the extent of LytB polymorphism, the lytB alleles from seven typical, clinical pneumococcal isolates of various serotypes and from 13 additional streptococci of the mitis group (12 atypical pneumococci and the Streptococcus mitis type strain) were sequenced [1].
LytB was purified by affinity chromatography, and its activity was suggested to be the first identified endo-beta-N-acetylglucosaminidase of Streptococcus pneumoniae [2].
Endo-beta-N-acetylglucosaminidase A (Endo A) from Arthrobacter protophormiae, the molecular mass of which is 72 kDa, had 32% sequence identity to Endo D, starting from the N-terminal sides of both enzymes, although Endo A hydrolyzes high-mannose-type oligosaccharides and does not hydrolyze complex type ones [3].

High impact information on lytB

The remaining genes included several virulence factors, such as capsular genes, iga, lytB, nanB, pspA, choline-binding proteins, and functions related to DNA acquisition, such as restriction-modification systems and comDE [4].
Specific inhibition of endo-beta-N-acetylglucosaminidase D by mannose and simple mannosides [5].
Molecular cloning and expression of endo-beta-N-acetylglucosaminidase D, which acts on the core structure of complex type asparagine-linked oligosaccharides [3].
New evidence of the substrate specificity of endo-beta-N-acetylglucosaminidase D [6].
These results indicated that endo-beta-N-acetylglucosaminidase D does not require the presence of a free hydroxyl group at the C-4 position of the alpha-mannosyl residue of the trisaccharide glycon: Man alpha 1----3Man beta 1----4GlcNAc beta 1---- [6].

References

Allelic variation of polymorphic locus lytB, encoding a choline-binding protein, from streptococci of the mitis group. Moscoso, M., Obregón, V., López, R., García, J.L., García, E. Appl. Environ. Microbiol. (2005) [Pubmed]
Purification and polar localization of pneumococcal LytB, a putative endo-beta-N-acetylglucosaminidase: the chain-dispersing murein hydrolase. De Las Rivas, B., García, J.L., López, R., García, P. J. Bacteriol. (2002) [Pubmed]
Molecular cloning and expression of endo-beta-N-acetylglucosaminidase D, which acts on the core structure of complex type asparagine-linked oligosaccharides. Muramatsu, H., Tachikui, H., Ushida, H., Song , X., Qiu, Y., Yamamoto, S., Muramatsu, T. J. Biochem. (2001) [Pubmed]
Relationship between codon biased genes, microarray expression values and physiological characteristics of Streptococcus pneumoniae. Martín-Galiano, A.J., Wells, J.M., de la Campa, A.G. Microbiology (Reading, Engl.) (2004) [Pubmed]
Specific inhibition of endo-beta-N-acetylglucosaminidase D by mannose and simple mannosides. Koide, N., Muramatsu, T. Biochem. Biophys. Res. Commun. (1975) [Pubmed]
New evidence of the substrate specificity of endo-beta-N-acetylglucosaminidase D. Mizuochi, T., Amano, J., Kobata, A. J. Biochem. (1984) [Pubmed]

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