@article {53,
	title = {Serine proteinases of the human body louse (Pediculus humanus): sequence characterization and expression patterns},
	journal = {Parasitology research},
	volume = {97},
	year = {2005},
	month = {2005},
	pages = {486 - 500},
	abstract = {After the previous characterization of one trypsin gene (Try1) of the human body louse Pediculus humanus, genes encoding a second trypsin (Try2) and a chymotrypsin (Chy1) have been cloned using degenerate serine proteinase primers and 5{\textquoteright}- and 3{\textquoteright}-RACE, and sequenced. The deduced 259 and 267 amino acid sequences of Try2 and Chy1 show an identity of 33\%-40\% to trypsinogens and chymotrypsinogens of other insects. Considering previously published partial sequences, P. humanus possesses at least one Try1 gene, five variants/isoforms of Try2 and six variants/isoforms of Chy1. The genomic DNA of Try2 contains three introns and Chy1 contains five introns. Using whole mount in situ hybridization, gene expression of Try1, Try2 and Chy1 has been localized not only in the distensible anterior region of the midgut of lice but sometimes also in the area following the distensible region. The Try2 gene was always expressed at much lower levels than Try1 or Chy1. This lower expression, the constitutive expression of Try1 and Chy1 at 1, 2, 6, 12 and 24 h after feeding of adults and the regional differences have been verified in quantitative real-time PCR.},
	isbn = {0932-0113},
	author = {Waniek,P. J. and Hendgen-Cotta,U. B. and Stock,P. and Mayer,C. and Kollien,A. H. and Schaub,G. A.}
}
@article {56,
	title = {Cloning and characterization of a trypsin-encoding cDNA of the human body louse Pediculus humanus},
	journal = {Insect Molecular Biology},
	volume = {13},
	year = {2004},
	note = {LR: 20041117; JID: 9303579; 0 (DNA Primers); EC 3.4.21.4 (Trypsin); ppublish},
	month = {2004},
	pages = {9 - 18},
	address = {England},
	abstract = {From a cDNA library of the whole insect, a trypsin gene of Pediculus humanus has been cloned and sequenced. The 908 bp clone has an open reading frame of 759 bp, which encodes a pre-proenzyme with 253 amino acid residues. A sixteen-residue N-terminal signal peptide is followed by a twelve-residue activation peptide with putative cleavage sites at Gly16 and Tyr28. The deduced amino acid sequence has several features typical of trypsin proteases and an overall identity of 35-43\% with the trypsins of several haematophagous Diptera. The 1.0 kb genomic trypsin gene contains three introns of 102, 79 and 80 nucleotides following the codons for Gly16, Gln74 and Ala155, respectively. Only a single gene seems to be present. In Northern blot analysis, unfed first instar larvae have an identical or slightly lower level of trypsin mRNA than fed adult lice, and in adults 2-24 h after the bloodmeal this gene shows a constitutive expression. After in vitro transcription and translation, the activation peptide is cleaved by chymotrypsin, a so far unreported phenomenon in trypsin activation.},
	keywords = {Amino Acids, animals, Base Sequence, Blotting, Northern, Comparative Study, dna, electrophoresis, genes, Molecular Sequence Data, Pediculus, polymerase, Research Support, Non-U.S. Gov{\textquoteright}t, sequence, Transition Temperature, Trypsin/genetics},
	isbn = {0962-1075},
	author = {Kollien,A. H. and Waniek,P. J. and Pr{\"o}ls,F. and Habedank,Birgit and Schaub,G. A.}
}
