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Articles by V Dubois
Total Records ( 2 ) for V Dubois
  C Arpin , C Quentin , F Grobost , E Cambau , J Robert , V Dubois , L Coulange , C Andre and on behalf of the Scientific Committee of ONERBA

The aim of this study was to assess the prevalence of the extended-spectrum β-lactamase (ESBL)-producing enterobacteria (ESBLE) in the French community, during a 2006 survey.


All enterobacteria isolated from urine samples of patients, exhibiting a decreased susceptibility to broad-spectrum cephalosporins, were analysed for their β-lactamase content (synergy test, isoelectrofocusing, conjugation transfer, PCR amplification and/or cloning experiments and sequencing). Additional co-resistances were investigated by PCR, sequencing and/or cloning. Epidemiological relationship was studied by PFGE for all species and, in addition, for Escherichia coli by the determination of the phylogenetic group, multilocus sequence type (ST) and O25b antigen. Characteristics of CTX-M-producing E. coli carriers were compared with other ESBLE carriers.


Seventy-two ESBLE were collected from 71 patients. Most of them expressed a CTX-M enzyme (n = 42, comprising 40 E. coli), with a predominance of CTX-M-15 (n = 24); 10 CTX-M-15-producing E. coli belonged to the same clone (phylogroup B2, ST131, serotype O25b). The 30 remaining strains possessed a TEM- or SHV-type ESBL. In addition, three strains presented unusual co-resistances such as DHA-1 (n = 2), QnrB4 and ArmA. Risk factors for ESBLE acquisition were substantially less frequent when the ESBL was of the CTX-M type, except for prior antimicrobial therapy. Eighteen percent of the patients were considered to have true community-acquired ESBLE; most of them harboured a CTX-M-producing E. coli.


This first nationwide study reports an ESBLE prevalence of 1.1% in the French community setting in 2006, mainly related to the presence of CTX-M-producing E. coli strains; furthermore, unusual co-resistances rarely found in the community setting were occasionally observed, which may threaten future emergence.

  V Dubois , C Van Ginneken , H De Cock , A. M Lambeir , P Van der Veken , K Augustyns , X Chen , S Scharpe and I. De Meester

The mRNA expression pattern of dipeptidyl peptidase (DPP) 8 and DPP9, two DPP4 homologs, was studied previously and showed a broad tissue distribution. In this study, protein expression and activity of DPP8 and DPP9 were investigated in male reproductive tissues of different mammals. Based on specific DPP activities and inhibition profiles, the proline-selective DPP activity in the bovine and rat testis could predominantly be attributed to DPP8/9 and not to DPP4. This is in contrast to the epididymis, where most of the activity was caused by DPP4. Bovine sperm preparations had very low or undetectable DPP8/9 activity. After characterization of polyclonal antibodies specific for DPP8 or DPP9, we could localize both enzymes in seminiferous tubules of the testis. A specific staining for DPP9 was found associated with spermatozoids embedded in the epithelium, just before their release into the lumen, and in spermatids. DPP8 was localized in spermatozoids in an earlier stage of maturation. These findings help to provide insight into the physiological role of DPP4-like enzymes in the male reproductive system. This manuscript contains online supplemental material at Please visit this article online to view these materials. (J Histochem Cytochem 57:531–541, 2009)

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