References of "Pastoret, Soumya"
     in
Bookmark and Share    
Full Text
Peer Reviewed
See detailDetection of disease resistance and susceptibility alleles in pigs using oligonucleotide microarray hybridization
Pastoret, Soumya; Ameels, Hélène; Bossiroy, Frédérique et al

in Journal of Veterinary Diagnostic Investigation (2012), 24(3), 479-488

A multiplex DNA microarray chip aimed at the identification of allelic polymorphisms was developed for simultaneous detection of swine disease resistance genes underlying malignant hyperthermia (RYR ... [more ▼]

A multiplex DNA microarray chip aimed at the identification of allelic polymorphisms was developed for simultaneous detection of swine disease resistance genes underlying malignant hyperthermia (RYR ), postweaning diarrhea, edema disease (FUT1), neonatal diarrhea (MUC4), and influenza (MX1). The on-chip detection was performed with fragmented polymerase chain reaction (PCR)-amplified products. Particular emphasis was placed on the reduction of the number of PCR reactions required. The targets were biotin labeled during the PCR reaction, and the arrays were detected using a colorimetric methodology. Target recognition was provided by specific capture probes designed for each susceptible or resistant allelic variant. Sequencing was chosen as the golden standard to assess chip’s accuracy. All genotypes retrieved from the microarray (476) fitted with sequencing data in spite of the fact that each pig was heterozygote for at least 1 target gene. [less ▲]

Detailed reference viewed: 66 (6 ULg)
Full Text
Peer Reviewed
See detailFunctional analysis of the cell division protein FtsW of Escherichia coli
Pastoret, Soumya; Fraipont, Claudine ULg; den Blaauwen, Tanneke et al

in Journal of Bacteriology (2004), 186(24), 8370-8379

Site-directed mutagenesis experiments combined with fluorescence microscopy shed light on the role of Escherichia coli FtsW, a membrane protein belonging to the SEDS family that is involved in ... [more ▼]

Site-directed mutagenesis experiments combined with fluorescence microscopy shed light on the role of Escherichia coli FtsW, a membrane protein belonging to the SEDS family that is involved in peptidoglycan assembly during cell elongation, division, and sporulation. This essential cell division protein has 10 transmembrane segments (TMSs). It is a late recruit to the division site and is required for subsequent recruitment of penicillin-binding protein 3 (PBP3) catalyzing peptide cross-linking. The results allow identification of several domains of the protein with distinct functions. The localization of PBP3 to the septum was found to be dependent on the periplasmic loop located between TMSs 9 and 10. The E240-A249 amphiphilic peptide in the periplasmic loop between TMSs 7 and 8 appears to be a key element in the functioning of FtsW in the septal peptidoglycan assembly machineries. The intracellular loop (containing the R166-FI78 amphiphilic peptide) between TMSs 4 and 5 and Gly 311 in TMS 8 are important components of the amino acid sequence-folding information. [less ▲]

Detailed reference viewed: 114 (11 ULg)
Full Text
Peer Reviewed
See detailStructural determinants required to target penicillin-binding protein 3 to the septum of Escherichia coli
Piette, André ULg; Fraipont, Claudine ULg; den Blaauwen, Tanneke et al

in Journal of Bacteriology (2004), 186(18), 6110-6117

In Escherichia coli, cell division is mediated by the concerted action of about 12 proteins that assemble at the division site to presumably form a complex called the divisome. Among these essential ... [more ▼]

In Escherichia coli, cell division is mediated by the concerted action of about 12 proteins that assemble at the division site to presumably form a complex called the divisome. Among these essential division proteins, the multimodular class B penicillin-binding protein 3 (PBP3), which is specifically involved in septall peptidoglycan synthesis, consists of a short intraceflular M1-R23 peptide fused to a F24-L39 membrane anchor that is linked via a G40-S70 peptide to an R71-1236 noncatalytic module itself linked to a D237-V577 catalytic penicillin -binding module. On the basis of localization analyses of PBP3 mutants fused to green fluorescent protein by fluorescence microscopy, it appears that the first 56 amino acid residues of PBP3 containing the membrane anchor and the G40-E56 peptide contain the structural determinants required to target the protein to the cell division site and that none of the putative protein interaction sites present in the noncatalytic module are essential for the positioning of the protein to the division site. Based on the effects of increasing production of FtsQ or FtsW on the division of cells expressing PBP3 mutants, it is suggested that these proteins could interact. We postulate that FtsQ could play a role in regulating the assembly of these division proteins at the division site and the activity of the peptidoglycan assembly machineries within the divisome. [less ▲]

Detailed reference viewed: 31 (8 ULg)