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1.
J Appl Microbiol ; 130(4): 1368-1379, 2021 Apr.
Article in English | MEDLINE | ID: mdl-32886839

ABSTRACT

AIM: To analyse the prevalence, genetic diversity and antimicrobial susceptibility of Campylobacter spp. in northern Spain. METHODS AND RESULTS: Campylobacter was isolated from 139 samples of broiler meat and faecal dropping of broiler and swine with a prevalence of 35·4, 62 and 42·8%, respectively. Campylobacter jejuni (n = 55) and Campylobacter coli (n = 31) were identified by multiplex-PCR in meat, faeces and human clinical samples while Campylobacter fetus (n = 3) was exclusively detected in the latter. Fingerprinting by flaA-RFLP and PFGE revealed 68 different genotypes from the 89 isolates with a Biodiversity Simpson's index of 0·98. The 86·5% of the isolates were resistant to ciprofloxacin, 85·4% to tetracycline and 49·4% to erythromycin; only three genotypes were susceptible to the three antimicrobial drugs. Multidrug resistance was detected in the 40·7% of the isolates. CONCLUSIONS: Campylobacter remains prevalent in northern Spain with a high biodiversity degree. About 93·3% of the isolates were resistant to one or more drugs. SIGNIFICANCE AND IMPACT OF THE STUDY: Although different measures are taken to control Campylobacter, the detection of isolates resistant to the drugs used in the treatment of campylobacteriosis is still high, including different species and genotypes. This evidences the need of additional strategies against this pathogen.


Subject(s)
Anti-Bacterial Agents/pharmacology , Campylobacter Infections/veterinary , Campylobacter coli/drug effects , Campylobacter jejuni/drug effects , Poultry Diseases/microbiology , Swine Diseases/microbiology , Animals , Campylobacter Infections/epidemiology , Campylobacter Infections/microbiology , Campylobacter coli/classification , Campylobacter coli/genetics , Campylobacter coli/isolation & purification , Campylobacter jejuni/classification , Campylobacter jejuni/genetics , Chickens , Ciprofloxacin/pharmacology , Drug Resistance, Bacterial , Erythromycin/pharmacology , Meat/microbiology , Microbial Sensitivity Tests , Molecular Typing , Phylogeny , Poultry Diseases/epidemiology , Prevalence , Spain/epidemiology , Swine , Swine Diseases/epidemiology , Tetracycline/pharmacology
2.
Int J Oral Maxillofac Surg ; 49(8): 1020-1028, 2020 Aug.
Article in English | MEDLINE | ID: mdl-31918988

ABSTRACT

After sagittal split osteotomy, the mandibular distal and proximal fragments do not always align themselves passively to one another, resulting in bony interferences and subsequent anomalous settlement of the condyles. Predicting these interferences could be an important ancillary procedure for avoiding intra- and postoperative surgical complications, rendering orthognathic surgery more effective and safer. This study evaluated the relevance of virtual surgical planning in assessing the displacement of the proximal segments after virtual distal segment repositioning, for predicting bony interferences between the segments and thus avoiding related intra- and postoperative surgical complications. The presence of interferences between the distal and proximal segments was compared between virtually predicted (computer-assisted simulation surgery, Dolphin software) and real cases in 100 consecutive patients diagnosed with dentofacial deformities who underwent orthognathic surgery with mandibular repositioning (using a short lingual osteotomy (SLO)). The results indicated that clockwise rotation of the mandible was the mandibular movement most prone to segment interference. Furthermore, virtual planning was sensitive (100%) but had low specificity (51.6%) in predicting proximal and distal segment interferences. This low specificity was due to the software-based automated design of the mandibular osteotomy, where the length of the distal segment was longer than the real SLO, and the mandibular ramus sagittal split was located just behind Spix's spine. Thus, more precise simulated osteotomies are needed to further validate the accuracy of virtual planning for this purpose.


Subject(s)
Orthognathic Surgical Procedures , Surgery, Computer-Assisted , Humans , Mandible , Mandibular Condyle , Mandibular Osteotomy , Osteotomy, Sagittal Split Ramus
3.
Aesthetic Plast Surg ; 43(2): 559-561, 2019 04.
Article in English | MEDLINE | ID: mdl-30725195

ABSTRACT

In the late years, the use of acellular dermal matrix (ADM) has extended rapidly in the field of breast reconstruction. However, with the follow-up visits, we discovered some deformities on the lateral part of the lower pole, due to the folding of the ADM. The aim of this letter is to share some tricks developed in our clinical practice that would permit the surgeon to avoid getting these irregularities in the aesthetic result of breast reconstruction with ADM. LEVEL OF EVIDENCE V: This journal requires that authors assign a level of evidence to each article. For a full description of these evidence-based medicine ratings, please refer to the Table of Contents or the online Instructions to Authors www.springer.com/00266 .


Subject(s)
Acellular Dermis , Breast Implants , Mammaplasty/methods , Humans
4.
Biochim Biophys Acta ; 1246(2): 128-34, 1995 Jan 19.
Article in English | MEDLINE | ID: mdl-7819279

ABSTRACT

Raman and Fourier transform infrared (FTIR) spectroscopies and circular dichroism (CD) have been applied to investigate the secondary structure of bombesin in the solid state and in phosphate buffer solution (pH 3.8). At concentrations around 10(-5) M, circular dichroism reveals that bombesin exists as an irregular or disordered conformation. However, the secondary structure of the peptide appears to be a mixture of disordered structure and intermolecular beta-sheets in 0.01 M sodium phosphate buffer when the peptide concentrations are higher than around 6.5 mM. The tendency of bombesin to form aggregated beta-sheet species seems to be originated mainly in the sequence of the residues 7-14, as supported by the Raman spectra and beta-sheet propensities (P beta) of the amino-acid residues. It is the hydrophobic force of this amino-acid sequence, and not a salt bridge effect, that is the factor responsible for the formation of peptide aggregates.


Subject(s)
Bombesin/chemistry , Protein Conformation , Amino Acid Sequence , Circular Dichroism , Molecular Sequence Data
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