Minimum structure of peptidoglycan required for induction of antibacterial protein synthesis in the silkworm, Bombyx mori

Various peptidoglycan fragments, different in mode of cross-linking and molecular size, were isolated, and the elicitor activity was tested for induction of antibacterial protein synthesis in larvae of Bombyx mori. Linear uncross-linked peptidoglycans from Bacillus licheniformis and Micrococcus lute...

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Bibliographic Details
Published in:Insect biochemistry and molecular biology 1999, Vol.29 (1), p.19-24
Main Authors: Iketani, Masao, Nishimura, Hitomi, Akayama, Koichi, Yamano, Yoshiaki, Morishima, Isao
Format: Article
Language:English
Subjects:
Animals
Anti-Infective Agents
Antibacterial protein induction
Bacillus licheniformis
Bombyx - immunology
Bombyx - metabolism
Bombyx mori
Cecropin
Insect Proteins - biosynthesis
Micrococcus luteus
N-Acetylglucosamine-N-acetylmuramic acid
peptidoglycan
Peptidoglycan - immunology
Peptidoglycan minimum structure
peptidoglycans
Silkworm
Structure-Activity Relationship
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Summary:Various peptidoglycan fragments, different in mode of cross-linking and molecular size, were isolated, and the elicitor activity was tested for induction of antibacterial protein synthesis in larvae of Bombyx mori. Linear uncross-linked peptidoglycans from Bacillus licheniformis and Micrococcus luteus were effective elicitors, similar to the directly cross-linked peptidoglycan from B. licheniformis cell wall. The fragments of uncross-linked peptidoglycan with a sugar chain length of four or more were active elicitors, but the disaccharide unit had no elicitor activity. The minimum structure of peptidoglycan required for induction of antibacterial protein synthesis was determined to be two repeating N-acetylglucosamine- N-acetylmuramic acid units with peptide side chains.
ISSN:0965-1748
1879-0240
DOI:10.1016/S0965-1748(98)00099-X