-
Something wrong with this record ?
The tick plasma lectin, Dorin M, is a fibrinogen-related molecule
Rego RO, Kovár V, Kopácek P, Weise C, Man P, Sauman I, Grubhoffer L.
Language English Country Great Britain
NLK
ScienceDirect (archiv)
from 1993-01-01 to 2009-12-31
- MeSH
- Financing, Organized MeSH
- Hemocytes chemistry MeSH
- Insect Proteins analysis physiology chemistry MeSH
- Cloning, Molecular MeSH
- Lectins physiology chemistry blood MeSH
- Molecular Sequence Data MeSH
- Ornithodoros metabolism MeSH
- Amino Acid Sequence MeSH
- Base Sequence MeSH
- Sequence Alignment MeSH
- Salivary Glands metabolism MeSH
- Protein Structure, Tertiary MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
A lectin, named Dorin M, previously isolated and characterized from the hemolymph plasma of the soft tick, Ornithodoros moubata, was cloned and sequenced. The immunofluorescence using confocal microscopy revealed that Dorin M is produced in the tick hemocytes. A tryptic cleavage of Dorin M was performed and the resulting peptide fragments were sequenced by Edman degradation and/or mass spectrometry. Two of three internal peptide sequences displayed a significant similarity to the family of fibrinogen-related molecules. Degenerate primers were designed and used for PCR with hemocyte cDNA as a template. The sequence of the whole Dorin M cDNA was completed by the method of RACE. The tissue-specific expression investigated by RT-PCR revealed that Dorin M, in addition to hemocytes, is significantly expressed in salivary glands. The derived amino-acid sequence clearly shows that Dorin M has a fibrinogen-like domain, and exhibited the most significant similarity with tachylectins 5A and 5B from a horseshoe crab, Tachypleus tridentatus. In addition, other protein and binding characteristics suggest that Dorin M is closely related to tachylectins-5. Since these lectins have been reported to function as non-self recognizing molecules, we believe that Dorin M may play a similar role in an innate immunity of the tick and, possibly, also in pathogen transmission by this vector.
- 000
- 00000naa 2200000 a 4500
- 001
- bmc07521379
- 003
- CZ-PrNML
- 005
- 20111210132819.0
- 008
- 090416s2006 xxk e eng||
- 009
- AR
- 040 __
- $a ABA008 $b cze $c ABA008 $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a xxk
- 100 1_
- $a Rego, Ryan O.
- 245 14
- $a The tick plasma lectin, Dorin M, is a fibrinogen-related molecule / $c Rego RO, Kovár V, Kopácek P, Weise C, Man P, Sauman I, Grubhoffer L.
- 314 __
- $a Institute of Parasitology, Academy of Sciences of the Czech Republic and Faculty of Biological Sciences, University of South Bohemia, Branisovská 31, Ceské Budejovice 370 05, Czech Republic.
- 520 9_
- $a A lectin, named Dorin M, previously isolated and characterized from the hemolymph plasma of the soft tick, Ornithodoros moubata, was cloned and sequenced. The immunofluorescence using confocal microscopy revealed that Dorin M is produced in the tick hemocytes. A tryptic cleavage of Dorin M was performed and the resulting peptide fragments were sequenced by Edman degradation and/or mass spectrometry. Two of three internal peptide sequences displayed a significant similarity to the family of fibrinogen-related molecules. Degenerate primers were designed and used for PCR with hemocyte cDNA as a template. The sequence of the whole Dorin M cDNA was completed by the method of RACE. The tissue-specific expression investigated by RT-PCR revealed that Dorin M, in addition to hemocytes, is significantly expressed in salivary glands. The derived amino-acid sequence clearly shows that Dorin M has a fibrinogen-like domain, and exhibited the most significant similarity with tachylectins 5A and 5B from a horseshoe crab, Tachypleus tridentatus. In addition, other protein and binding characteristics suggest that Dorin M is closely related to tachylectins-5. Since these lectins have been reported to function as non-self recognizing molecules, we believe that Dorin M may play a similar role in an innate immunity of the tick and, possibly, also in pathogen transmission by this vector.
- 650 _2
- $a sekvence aminokyselin $7 D000595
- 650 _2
- $a zvířata $7 D000818
- 650 _2
- $a sekvence nukleotidů $7 D001483
- 650 _2
- $a klonování DNA $7 D003001
- 650 _2
- $a hemocyty $x chemie $7 D006434
- 650 _2
- $a hmyzí proteiny $x analýza $x fyziologie $x chemie $7 D019476
- 650 _2
- $a lektiny $x fyziologie $x chemie $x krev $7 D037102
- 650 _2
- $a molekulární sekvence - údaje $7 D008969
- 650 _2
- $a Ornithodoros $x metabolismus $7 D026861
- 650 _2
- $a terciární struktura proteinů $7 D017434
- 650 _2
- $a slinné žlázy $x metabolismus $7 D012469
- 650 _2
- $a sekvenční seřazení $7 D016415
- 650 _2
- $a financování organizované $7 D005381
- 700 1_
- $a Kovář, Vojtěch. $7 _AN030738
- 700 1_
- $a Kopáček, Petr, $d 1958- $7 _AN030739
- 700 1_
- $a Weise, Christoph
- 700 1_
- $a Man, Petr $7 xx0131981
- 700 1_
- $a Šauman, Ivo
- 700 1_
- $a Grubhoffer, Libor, $d 1957- $7 xx0021786
- 773 0_
- $w MED00004948 $t Insect biochemistry and molecular biology $g Roč. 36, č. 4 (2006), s. 291-299 $x 0965-1748
- 910 __
- $a ABA008 $b x $y 9
- 990 __
- $a 20090312170439 $b ABA008
- 991 __
- $a 20090717113121 $b ABA008
- 999 __
- $a ok $b bmc $g 644219 $s 497100
- BAS __
- $a 3
- BMC __
- $a 2006 $b 36 $c 4 $d 291-299 $i 0965-1748 $m Insect biochemistry and molecular biology $x MED00004948
- LZP __
- $a 2009-B1/vtme