rdf:type |
|
lifeskim:mentions |
umls-concept:C0006556,
umls-concept:C0009015,
umls-concept:C0015576,
umls-concept:C0026584,
umls-concept:C0086022,
umls-concept:C0205409,
umls-concept:C0322859,
umls-concept:C0441655,
umls-concept:C0442335,
umls-concept:C0597874,
umls-concept:C0680022,
umls-concept:C1136254,
umls-concept:C1515670,
umls-concept:C1705099,
umls-concept:C2827424
|
pubmed:issue |
29
|
pubmed:dateCreated |
1999-8-19
|
pubmed:abstractText |
An antimicrobial peptide belonging to the cecropin family was isolated from the hemolymph of bacteria-challenged adult Aedes aegypti. This new peptide, named cecropin A, was purified to homogeneity and fully characterized after cDNA cloning. The 34-residue A. aegypti cecropin A is different from the majority of reported insect cecropins in that it is devoid of a tryptophan residue and C-terminal amidation. The importance of these two structural features on the activity spectrum was investigated using a chemically synthesized peptide. A comparison of the antimicrobial activity spectrum of A. aegypti and Drosophila cecropin A showed a lower activity for the mosquito molecule. A. aegypti cecropin mRNA expression was not detected by Northern blot or reverse transcription-polymerase chain reaction analysis in any immature stage of the mosquito, nor in naïve adults, but it was observed in challenged adults 6 h after bacteria inoculation, and it continued over 7-10 days.
|
pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
0021-9258
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
16
|
pubmed:volume |
274
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
20092-7
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:10400619-Aedes,
pubmed-meshheading:10400619-Amino Acid Sequence,
pubmed-meshheading:10400619-Animals,
pubmed-meshheading:10400619-Anti-Bacterial Agents,
pubmed-meshheading:10400619-Antimicrobial Cationic Peptides,
pubmed-meshheading:10400619-Base Sequence,
pubmed-meshheading:10400619-Blotting, Northern,
pubmed-meshheading:10400619-Cloning, Molecular,
pubmed-meshheading:10400619-DNA, Complementary,
pubmed-meshheading:10400619-Hemolymph,
pubmed-meshheading:10400619-Molecular Sequence Data,
pubmed-meshheading:10400619-Peptides,
pubmed-meshheading:10400619-Phylogeny,
pubmed-meshheading:10400619-RNA, Messenger,
pubmed-meshheading:10400619-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:10400619-Sequence Homology, Amino Acid
|
pubmed:year |
1999
|
pubmed:articleTitle |
Antimicrobial activity spectrum, cDNA cloning, and mRNA expression of a newly isolated member of the cecropin family from the mosquito vector Aedes aegypti.
|
pubmed:affiliation |
Animal Health and Biomedical Sciences, University of Wisconsin, Madison, Wisconsin 53706, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|