State-of-the-art three-dimensional analysis of soft tissue changes following Le Fort I maxillary advancement

We describe the comprehensive 3-dimensional analysis of facial changes after Le Fort I osteotomy and introduce a new tool for anthropometric analysis of the face. We studied the cone-beam computed tomograms of 33 patients taken one month before and 6-12 months after Le Fort I maxillary advancement with or without posterior vertical impaction. Use of a generic facial mesh for dense correspondence analysis of changes in the soft tissue showed a mean (SD) anteroposterior advancement of the maxilla of 5.9 (1.7) mm, and mean (SD) minimal anterior and posterior vertical maxillary impaction of 0.1 (1.7) mm and 0.6 (1.45) mm, respectively. It also showed distinctive forward and marked lateral expansion around the upper lip and nose, and pronounced upward movement of the alar curvature and columella. The nose was widened and the nostrils advanced. There was minimal forward change at the base of the nose (subnasale and alar base) but a noticeable upward movement at the nasal tip. Changes at the cheeks were minimal. Analysis showed widening of the midface and upper lip which, to our knowledge, has not been reported before. The nostrils were compressed and widened, and the lower lip shortened. Changes at the chin and lower lip were secondary to the limited maxillary impaction

Protein Glycosylation in Helicobacter pylori: Beyond the Flagellins?

Glycosylation of flagellins by pseudaminic acid is required for virulence in Helicobacter pylori. We demonstrate that, in H. pylori, glycosylation extends to proteins other than flagellins and to sugars other than pseudaminic acid. Several candidate glycoproteins distinct from the flagellins were detected via ProQ-emerald staining and DIG- or biotin- hydrazide labeling of the soluble and outer membrane fractions of wild-type H. pylori, suggesting that protein glycosylation is not limited to the flagellins. DIG-hydrazide labeling of proteins from pseudaminic acid biosynthesis pathway mutants showed that the glycosylation of some glycoproteins is not dependent on the pseudaminic acid glycosylation pathway, indicating the existence of a novel glycosylation pathway. Fractions enriched in glycoprotein candidates by ion exchange chromatography were used to extract the sugars by acid hydrolysis. High performance anion exchange chromatography with pulsed amperometric detection revealed characteristic monosaccharide peaks in these extracts. The monosaccharides were then identified by LC-ESI-MS/MS. The spectra are consistent with sugars such as 5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-L-manno-nonulosonic acid (Pse5Ac7Ac) previously described on flagellins, 5-acetamidino-7-acetamido-3,5,7,9-tetradeoxy-L-glycero-L-manno-nonulosonic acid (Pse5Am7Ac), bacillosamine derivatives and a potential legionaminic acid derivative (Leg5AmNMe7Ac) which were not previously identified in H. pylori. These data open the way to the study of the mechanism and role of protein glycosylation on protein function and virulence in H. pylori