Molecular cloning, structure and bait region splice variants of α2-macroglobulin from the soft tick Ornithodoros moubata

2003 ◽  
Vol 33 (8) ◽  
pp. 841-851 ◽  
Author(s):  
Thangamani Saravanan ◽  
Christoph Weise ◽  
Daniel Sojka ◽  
Petr Kopáček
Keyword(s):  
Molecular Cloning ◽  
Splice Variants ◽  
Soft Tick ◽  
Ornithodoros Moubata ◽  
Bait Region ◽  
Α2 Macroglobulin

Molecular cloning and comparative analysis of fibrinogen-related proteins from the soft tick Ornithodoros moubata and the hard tick Ixodes ricinus

2005 ◽  
Vol 35 (9) ◽  
pp. 991-1004 ◽  
Author(s):  
Ryan O.M. Rego ◽  
Ondřej Hajdušek ◽  
Vojtěch Kovář ◽  
Petr Kopáček ◽  
Libor Grubhoffer ◽  
...  
Keyword(s):  
Comparative Analysis ◽  
Molecular Cloning ◽  
Ixodes Ricinus ◽  
Hard Tick ◽  
Soft Tick ◽  
Ornithodoros Moubata ◽  
Related Proteins

scholarly journals Development of selective protease inhibitors via engineering of the bait region of human α2-macroglobulin

2021 ◽  
pp. 100879
Author(s):  
Seandean Lykke Harwood ◽  
Nadia Sukusu Nielsen ◽  
Khang Diep ◽  
Kathrine Tejlgård Jensen ◽  
Peter Kresten Nielsen ◽  
...  
Keyword(s):  
Protease Inhibitors ◽  
Bait Region ◽  
Α2 Macroglobulin

Antibacterial peptide defensin is involved in midgut immunity of the soft tick, Ornithodoros moubata

2002 ◽  
Vol 11 (6) ◽  
pp. 611-618 ◽  
Author(s):  
Y. Nakajima ◽  
A. van der Goes van Naters-Yasui ◽  
D. Taylor ◽  
M. Yamakawa
Keyword(s):  
Antibacterial Peptide ◽  
Soft Tick ◽  
Ornithodoros Moubata

scholarly journals Structural and functional insights into Escherichia coli α2-macroglobulin endopeptidase snap-trap inhibition

2015 ◽  
Vol 112 (27) ◽  
pp. 8290-8295 ◽  
Author(s):  
Irene Garcia-Ferrer ◽  
Pedro Arêde ◽  
Josué Gómez-Blanco ◽  
Daniel Luque ◽  
Stephane Duquerroy ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Envelope ◽  
Large Cell ◽  
Structural Rearrangement ◽  
Gram Negative Bacteria ◽  
Human Gut ◽  
Bait Region ◽  
Α2 Macroglobulin ◽  
Thioester Bond ◽  
Peptidase Inhibitor

The survival of commensal bacteria requires them to evade host peptidases. Gram-negative bacteria from the human gut microbiome encode a relative of the human endopeptidase inhibitor, α2-macroglobulin (α2M). Escherichia coli α2M (ECAM) is a ∼180-kDa multidomain membrane-anchored pan-peptidase inhibitor, which is cleaved by host endopeptidases in an accessible bait region. Structural studies by electron microscopy and crystallography reveal that this cleavage causes major structural rearrangement of more than half the 13-domain structure from a native to a compact induced form. It also exposes a reactive thioester bond, which covalently traps the peptidase. Subsequently, peptidase-laden ECAM is shed from the membrane and may dimerize. Trapped peptidases are still active except against very large substrates, so inhibition potentially prevents damage of large cell envelope components, but not host digestion. Mechanistically, these results document a novel monomeric “snap trap.”

Molecular cloning, expression and isolation of ferritins from two tick species—Ornithodoros moubata and Ixodes ricinus

2003 ◽  
Vol 33 (1) ◽  
pp. 103-113 ◽  
Author(s):  
Petr Kopáček ◽  
Jana Ždychová ◽  
Toyoshi Yoshiga ◽  
Christoph Weise ◽  
Natasha Rudenko ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Ixodes Ricinus ◽  
Tick Species ◽  
Ornithodoros Moubata
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