The revascularisation and remodelling of allografts used to replace the anterior cruciate ligament in the canine knee were studied by microangiographic, histological and biomechanical methods. The 26 allografts were obtained from the patellar tendons of other dogs and were stored by deep freezing. In a control study a strip of patellar tendon from the same leg was used as an autologous free graft. Microangiography showed that the allografts had been revascularised from the sixth postoperative week, and had later developed an intrinsic vascular pattern similar to that of a normal anterior cruciate ligament. Histologically, the allograft regained a fibrous framework similar to that of a normal ligament, and showed no evidence of immunological rejection. Biomechanical tests on the allograft replacements showed that their mean maximum tensile strength at 30 weeks was about 30% of that of the control ligaments. There were no significant differences between the mechanical properties of the allografts and the autografts.

SummaryA glycosylation island is a genetic region required for glycosylation. The glycosylation island of flagellin in Pseudomonas syringae pv. tabaci 6605 consists of three orfs : orf1 , orf2 and orf3 . Orf1 and orf2 encode putative glycosyltransferases, and their deletion mutants, D orf1 and D orf2 , exhibit deficient flagellin glycosylation or produce partially glycosylated flagellin respectively. Digestion of glycosylated flagellin from wild-type bacteria and non-glycosylated flagellin from D orf1 mutant using aspartic N -peptidase and subsequent HPLC analysis revealed candidate glycosylated amino acids. By generation of site-directed Ser/Ala-substituted mutants, all glycosylated amino acid residues were identified at positions 143, 164, 176, 183, 193 and 201. Matrix-assisted laser desorption/ionization time of flight (MALDI-TOF) mass spectrometry (MS) analysis revealed that each glycan was about 540 Da. While all glycosylation-defective mutants retained swimming ability, swarming ability was reduced in the D orf1 , D orf2 and Ser/Ala-substituted mutants. All glycosylation mutants were also found to be impaired in the ability to adhere to a polystyrene surface and in the ability to cause disease in tobacco. Based on the predicted tertiary structure of flagellin, S176 and S183 are expected to be located on most external surface of the flagellum. Thus the effect of Ala-substitution of these serines is stronger than that of other serines. These results suggest that glycosylation of flagellin in P. syringae pv. tabaci 6605 is required for bacterial virulence. It is also possible that glycosylation of flagellin may mask elicitor function of flagellin molecule.

No abstract

No abstract

No abstract