Kekropiinit- hyönteisten kehon muodostamia puolustuspeptideitä, jotka pystyvät tekemään biologisiin kalvoihin aukon.

 Tämä asia on nyt hyönteisten peptidien puolelta, mutta näillä itikat saavat aikaan omaa vastustuskykyä  virusta vastaan.Esim dengue -virus aiheuttaa että itikassa kehittyy jotain defensiiniå, peptidiä, ja se peptidi taas ilmenee  itikan pureman yhteydessä itikan syljessä, ja ehkä  pystyy tekemään reiän johonkin  infektioketjussa tarvittavaan kohtaa. Mikä suhde  DENV viruksella ja sen vektorihyönteisellä sitten on, molemmat ainakin lisääntyvät ihmisen kustannuksella.

Cecropin

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Cecropin family
Identifiers
Symbol	Cecropin
Pfam	PF00272
InterPro	IPR000875
PROSITE	PDOC00241
SCOP	1f0d
SUPERFAMILY	1f0d
TCDB	1.C.17
OPM superfamily	160
OPM protein	1d9j
[show]Available protein structures:

Cecropins are antimicrobial peptides.^[1][2] They were first isolated from the hemolymph of Hyalophora cecropia, from whence the term cecropin was derived. Cecropins lyse bacterial cell membranes; they also inhibit proline uptake and cause leaky membranes.
Cecropins^[3][4][5] constitute a main part of the cell-free immunity of insects. Cecropins are small proteins of about 31 - 37 amino acid residues active against both Gram-positive and Gram-negative bacteria. Cecropins isolated from insects other than Hyalophora cecropia (Cecropia moth) have been given various names; bactericidin, lepidopteran, sarcotoxin, etc. All of these peptides are structurally related. Cecropin P1, an intestinal antibacterial peptide from Sus scrofa (Pig), also belongs to this family. Cecropin family also consists Cecropin A and Cecropin B.
Cecropin is an anticancer polypeptide(L). Structure consists of mainly alpha helixes, determined by solution NMR. Protein molecular weight = 4203.4g/mol.^[6] At low peptide to lipid ratios ion channels are formed, at high peptide to lipid ratios pores are formed.^[7]
 

• ^{DENGUE-virus  ja sen itikassa aiheuttama  ITIKAN DEFENSIINI} 

  Induction of a peptide with activity against a broad spectrum of pathogens in the Aedes aegypti salivary gland, following Infection with Dengue Virus.

  Luplertlop N, Surasombatpattana P, Patramool S, Dumas E, Wasinpiyamongkol L, Saune L, Hamel R, Bernard E, Sereno D, Thomas F, Piquemal D, Yssel H, Briant L, Missé D.

  PLoS Pathog. 2011 Jan 13;7(1):e1001252. doi: 10.1371/journal.ppat.1001252.

  PMID:

  21249175

  [PubMed - indexed for MEDLINE]

  Free PMC Article

  •  

  Related citations
  Select item 190850243.

  In-silico homology modeling of three isoforms of insect defensins from the dengue vector mosquito, Aedes aegypti (Linn., 1762).

  Dhananjeyan KJ, Sivaperumal R, Paramasivan R, Thenmozhi V, Tyagi BK.

  J Mol Model. 2009 May;15(5):507-14. doi: 10.1007/s00894-008-0408-7. Epub 2008 Dec 16.

  PMID:

  19085024

  [PubMed - indexed for MEDLINE]

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