Isolation and characterization of the lysozyme-encoding gene from the silkworm Bombyx mori

Isolation and characterization of the lysozyme-encoding gene from the silkworm Bombyx mori

We have isolated and characterized a Bombyx mori (Bm) cDNA encoding a lysozyme (Lyz). A 90-bp DNA fragment was amplified by PCR using degenerate oligodeoxyribonucleotide primers derived from the known amino acid (aa) sequence of the Bm Lyz. These PCR fragments were used to screen a rat body cDNA lib...

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Veröffentlicht in:Gene 1995-08, Vol.161 (2), p.199-203
Hauptverfasser: Lee, Won-Jae, Brey, Paul T.
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acid Sequence
amino acid sequences
Animals
Bacillus licheniformis
Base Sequence
Bombyx - enzymology
Bombyx - genetics
Bombyx mori
cDNA cloning
Chickens
complementary DNA
cuticle
defense
defense mechanisms
DNA, Complementary - genetics
Enzyme Precursors - genetics
epidermis
evolution
experimental infections
fat body
genbank/l37416
gene expression
Genes, Insect
hemocytes
Insect immunity
lys gene
lysozyme
messenger RNA
Molecular Sequence Data
Muramidase - genetics
nucleotide sequences
Polymerase Chain Reaction
RNA, Messenger - genetics
RNA, Messenger - metabolism
sequence analysis
Sequence Homology, Amino Acid
structural genes
up-regulation
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Beschreibung
Zusammenfassung:We have isolated and characterized a Bombyx mori (Bm) cDNA encoding a lysozyme (Lyz). A 90-bp DNA fragment was amplified by PCR using degenerate oligodeoxyribonucleotide primers derived from the known amino acid (aa) sequence of the Bm Lyz. These PCR fragments were used to screen a rat body cDNA library. A clone containing the complete lys cDNA (1294 bp) was isolated and completely sequenced. The deduced 137-aa sequence showed high homology with other chicken-type Lyz. Bm lys gene expression was constitutive in fat body, cuticular epidermal tissue and at a very low level in hemocytes. This gene expression was up-regulated in fat body, hemocytes and cuticular epidermal tissue following the injection of Gram + bacteria.
ISSN:0378-1119
1879-0038
DOI:10.1016/0378-1119(95)00199-G