Nucleic acid encoding endolysin fusion protein

Details Nucleic acid encoding endolysin fusion protein Nucleic acid encoding endolysin fusion protein

2005-12-05

2009-08-11

Prouty, Rebecca E (Department: 1656)

Chemistry: molecular biology and microbiology

Micro-organism, tissue cell culture or enzyme using process...

Recombinant dna technique included in method of making a...

C536S023200, C536S023400, C536S023700, C536S023100, C435S252300, C435S254110, C435S254200, C435S325000, C435S419000, C435S069100, C435S440000, C435S070100, C435S071100, C435S320100

Reexamination Certificate

active

07572602

ABSTRACT:
The invention concerns a recombinant nucleic acid molecule encoding an antimicrobial fusion peptidoglycan endopeptidase. The recombinant nucleic acid molecule according to the invention is formed from a nucleic acid encoding a bacterial endopeptidase (lysostaphin) fromStaphylococcus simulansand a nucleic acid encoding a second endopeptidase (endolysin) module from Group B streptococcal bacteriophage B30. The encoded fusion endopeptidase has antimicrobial activity and kills bothStaphylococcusbacteria andStreptococcusbacteria.

REFERENCES:
Croux C., Ronda C., Lopez R., and Garcia J.L., Interchage of functional domains switches enzyme specificity: construction of a chimeric pneumococcal-clostridial cell wall lytic enzyme, 1993, 9(5): 1019-1025.
Ngo et al. in The Protein Folding Problem and Tertiary Structure Prediction, 1994, Merz et al. (ed.), Birkhauser, Boston, MA, pp. 433 and 492-495.
Bateman, Alex et al., “The Chap domain: a large family or amidases including GSP amidase and peptidoglycan hydrolases,”Trends in Biochemical Sciences, May 2003, vol. 28, No. 5, pp. 234-237.
Heinrich, Peter et al., “The Molecular organization of the lysostaphin gene and its sequences repeated in tandern,”MGG, 1987, vol. 209, pp. 563-569.
Pritchard, David et al., “The bifunctional peptidoglycan lysine ofStreptococcus agalactiaebacteriophage B30,”Microbiology, 2004, vol. 150, pp. 2079-2087.
Rigden, Daniel J. et al., “Amidase domains from bacterial and phage autolysins define a family of y-d, L-glutamate-specific amidohydrolases,”Trends in Biochemical Sciences, May 2003, vol. 28, No. 5, pp. 230-234.

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