References of "Thiry, M"
     in
Bookmark and Share    
Peer Reviewed
See detailA recombinant viral haemorrhagic septicaemia virus glycoprotein expressed in insect cells induces protective immunity in rainbow trout
Lecocq-Xhonneux, F.; Thiry, M.; Dheur, I. et al

in Journal of General Virology (The) (1994), 75

Viral haemorrhagic septicaemia (VHS) is a fish rhabdovirus infection of world-wide importance. Control policies have been established but the disease still causes heavy losses in fish farming. The ... [more ▼]

Viral haemorrhagic septicaemia (VHS) is a fish rhabdovirus infection of world-wide importance. Control policies have been established but the disease still causes heavy losses in fish farming. The development of a recombinant subunit vaccine was initiated to produce a safe and effective vaccine to protect fish against VHS. The VHS virus (VHSV) glycoprotein, which induces neutralizing antibodies in rainbow trout, was chosen for expression in insect cells using a baculovirus vector. The Mr of the recombinant protein estimated by SDS-PAGE was slightly lower than that of the native viral protein. The recombinant protein displayed different degrees of glycosylation and was recognized in ELISA by neutralizing antibodies. It was transported to the plasma membrane of insect cells where its ability to induce membrane fusion was preserved. The efficacy of the recombinant protein as a vaccine was compared with those of an inactivated and an attenuated vaccine. When injected intraperitoneally into rainbow trout, the baculo-virus-encoded protein was shown (i) to induce the synthesis of VHSV-neutralizing antibodies and (ii) to confer protection against virus challenge. Immunization performed by immersion failed. This is the first report of a recombinant vaccine that protects fish against VHSV. [less ▲]

Detailed reference viewed: 16 (0 ULg)
Full Text
Peer Reviewed
See detailModification ultrastructurale du nucléole au cours de l'ovogenèse chez un poisson téléostéen ovipare Barbus barbus.
Thiry, M.; Lepoint, A.; Poncin, Pascal ULg et al

in Cahiers d'Ethologie Appliquée (1993), 13(2), 247-248

Detailed reference viewed: 31 (6 ULg)
Full Text
Peer Reviewed
See detailCloning and Expression in Escherichia Coli of Three Lipase-Encoding Genes from the Psychrotrophic Antarctic Strain Moraxella Ta144
Feller, Georges ULg; Thiry, M.; Arpigny, J. L. et al

in Gene (1991), 102(1), 111-5

The cloning and expression of genes from a psychrotrophic bacterium in a mesophilic host are described. Three lipase (Lip)-encoding genes (lip) from the antarctic psychrotroph, Moraxella TA144, were ... [more ▼]

The cloning and expression of genes from a psychrotrophic bacterium in a mesophilic host are described. Three lipase (Lip)-encoding genes (lip) from the antarctic psychrotroph, Moraxella TA144, were cloned by inserting Sau3AI-generated DNA fragments into the BamHI site of the pSP73 plasmid vector. To prevent heat denaturation of the gene product, the screening procedure on agar plates containing an emulsified lipid involved growing of Escherichia coli recombinant colonies at 25 degrees C followed by incubation at 0 degree C. The three recombinant (reLip) were cell-associated and differed by their respective specificity towards p-nitrophenyl esters of various aliphatic chain lengths. These cloned reLip conserved the main character of the wild-type enzymes, i.e. a dramatic shift of the optimal temperature of activity towards low temperatures and pronounced heat lability. [less ▲]

Detailed reference viewed: 15 (0 ULg)
Full Text
Peer Reviewed
See detailNucleotide Sequence of the Lipase Gene Lip2 from the Antarctic Psychrotroph Moraxella Ta144 and Site-Specific Mutagenesis of the Conserved Serine and Histidine Residues
Feller, Georges ULg; Thiry, M.; Gerday, Charles ULg

in DNA & Cell Biology (1991), 10(5), 381-8

The lip2 gene from the antarctic psychotroph Moraxella TA144 was sequenced. The primary structure of the Lip2 preprotein deduced from the nucleotide sequence is composed of 433 amino acids with a ... [more ▼]

The lip2 gene from the antarctic psychotroph Moraxella TA144 was sequenced. The primary structure of the Lip2 preprotein deduced from the nucleotide sequence is composed of 433 amino acids with a predicted Mr of 47,222. This enzyme contains a Ser-centered consensus sequence and a conserved His-Gly dipeptide found in most lipase amino-terminal domains. These sequences are involved in the lipase active site conformation since substitution of the conserved Ser or His residues by Ala and Gln, respectively, results in the loss of both lipase and esterase activities. Structural factors that would allow proper enzyme flexibility at low temperatures are discussed. It is suggested that only subtle changes in the primary structure of these psychrotrophic enzymes can account for their ability to catalyze lipolysis at temperatures close to 0 degrees C. [less ▲]

Detailed reference viewed: 19 (2 ULg)
Full Text
Peer Reviewed
See detailNucleotide Sequence of the Lipase Gene Lip3 from the Antarctic Psychotroph Moraxella Ta144
Feller, Georges ULg; Thiry, M.; Gerday, Charles ULg

in Biochimica et Biophysica Acta (1991), 1088(2), 323-4

A lipase gene (lip3) from the psychotrophic strain Moraxella TA144 has been cloned and sequenced. The deduced primary structure of the lipase preprotein is composed of 315 amino acids with a predicted Mr ... [more ▼]

A lipase gene (lip3) from the psychotrophic strain Moraxella TA144 has been cloned and sequenced. The deduced primary structure of the lipase preprotein is composed of 315 amino acids with a predicted Mr of 34,772. This enzyme contains two consensus peptides showing cluster of glycine residues that may be involved in domain flexibility. The cloned gene product conserves the low temperature activity and the thermolability properties of the wild enzyme. [less ▲]

Detailed reference viewed: 8 (0 ULg)
Full Text
Peer Reviewed
See detailSequence of a Lipase Gene from the Antarctic Psychrotroph Moraxella Ta144
Feller, Georges ULg; Thiry, M.; Gerday, Charles ULg

in Nucleic Acids Research (1990), 18(21), 6431

Detailed reference viewed: 13 (0 ULg)
Full Text
Peer Reviewed
See detailLIPASES FROM PSYCHROTROPHIC ANTARCTIC BACTERIA
Feller, Georges ULg; Thiry, M.; Arpigny, J. L. et al

in FEMS Microbiology Letters (1990), 66(1-3), 239-243

Detailed reference viewed: 40 (1 ULg)