Caudal cruciate ligament avulsion at its origin in a dog

Η ρήξη του οπίσθιου χιαστού συνδέσμου είναι σπάνια στον σκύλο και συνήθως συνυπάρχει με ταυτό-χρονη ρήξη του πρόσθιου χιαστού συνδέσμου. Ένας ημίαιμος σκύλος ηλικίας 10 μηνών προσκομίστηκε με χωλότητα του οπίσθιου δεξιού άκρου. Η ορθοπαιδική εξέταση αποκάλυψε θετική προσθιοπίσθια συρταρωτή κίνηση στο δεξιό γόνατο. Η αρθροτομή επιβεβαίωσε τη ρήξη του πρόσθιου χιαστού συνδέσμου και έδειξε και απόσπαση του οπίσθιου χιαστού συνδέσμου στην πρόσφυσή του. Το γόνατο σταθεροποιήθηκε με τη χρήση εξωαρθρικής τεχνικής (νάιλον ράμμα μεταξύ έξω σησαμοειδούς και κνημιαίου κυρτώματος). Οκτώ μήνες μετεγχειρητικά ο σκύλος δεν παρουσίαζε εμφανή χωλότητα και παραμένει έτσι μέχρι και την τελευταία επανεξέταση (3 χρόνια). Το περιστατικό αυτό εγείρει την πιθανότητα ότι η αποκατάσταση της λειτουργίας του οπίσθιου χιαστού συνδέσμου δεν είναι πάντα απαραίτητη για την επιτυχή έκβαση των ζώων.Caudal cruciate ligament (CaCL) rupture is uncommon in dogs and usually occurs with a concurrent rupture of the cranial cruciate ligament (CrCL). A 10-month-old cross-bred dog was presented with left hind limb lameness. Orthopaedic examination revealed positive craniocaudal drawer sign in the left stifle. Arthrotomy confirmed CrCL rupture, and showed CaCL avulsion fracture at its origin. The stifle was stabilized using extracapsular lateral fabellotibial suture. Eight months postoperatively the dog was free of obvious lameness and remained sound until the last re-evaluation (3 years). This case raises the possibility that restoration of the CaCL function is not always essential for animals’ successful outcome

The ϕ6 Cystovirus Protein P7 Becomes Accessible to Antibodies in the Transcribing Nucleocapsid: A Probe for Viral Structural Elements

Protein P7 is a component of the cystovirus viral polymerase complex. In the unpackaged procapsid, the protein is situated in close proximity to the viral directed RNA polymerase, P2. Cryo-electron microscopy difference maps from the species ϕ6 procapsid have demonstrated that P7 and P2 likely interact prior to viral RNA packaging. The location of P7 in the post-packaged nucleocapsid (NC) remains unknown. P7 may translocate closer to the five-fold axis of a filled procapsid but this has not been directly visualized. We propose that monoclonal antibodies (Mabs) can be selected that serve as probe- reagents for viral assembly and structure. A set of Mabs have been isolated that recognize and bind to the ϕ6 P7. The antibody set contains five unique Mabs, four of which recognize a linear epitope and one which recognizes a conformational epitope. The four unique Mabs that recognize a linear epitope display restricted utilization of Vκ and VH genes. The restricted genetic range among 4 of the 5 antibodies implies that the antibody repertoire is limited. The limitation could be the consequence of a paucity of exposed antigenic sites on the ϕ6 P7 surface. It is further demonstrated that within ϕ6 nucleocapsids that are primed for early-phase transcription, P7 is partially accessible to the Mabs, indicating that the nucleocapsid shell (protein P8) has undergone partial disassembly exposing the protein’s antigenic sites

Loss of tolerance to gut immunity protein; glycoprotein 2 (GP2) is associated with progressive disease course in primary sclerosing cholangitis

Abstract Glycoprotein 2[GP2] is a specific target of pancreatic autoantibodies[PAbs] in Crohn’s disease(CD) and is involved in gut innate immunity processes. Our aim was to evaluate the prevalence and prognostic potential of PAbs in primary sclerosing cholangitis(PSC). Sixty-five PSC patients were tested for PAbs by indirect immunofluorescence and compared with healthy (n = 100) and chronic liver disease controls(CLD, n = 488). Additionally, a panel of anti-microbial antibodies and secretory (s)IgA levels were measured, as markers of bacterial translocation and immune dysregulation. PAbs were more frequent in PSC(46.2%) compared to controls(healthy:0% and CLD:4.5%), [P < 0.001, for each]. Occurrence of anti-GP2 antibody was 30.8% (20/65) and was exclusively of IgA isotype. Anti-GP2 IgA positive patients had higher sIgA levels (P = 0.021). With flow-cytometry, 68.4% (13/19) of anti-GP2 IgA antibodies were bound with secretory component, suggesting an active retro-transportation of anti-GP2 from the gut lumen to the mucosa. Anti-GP2 IgA was associated with shorter transplant-free survival [PLogRank < 0.01] during the prospective follow-up (median, IQR: 87 [9–99] months) and remained an independent predictor after adjusting for Mayo risk score(HR: 4.69 [1.05–21.04], P = 0.043). These results highlight the significance of gut-liver interactions in PSC. Anti-GP2 IgA might be a valuable tool for risk stratification in PSC and considered as a potential therapeutic target

Neutralising Antibodies against Ricin Toxin

The Centers for Disease Control and Prevention have listed the potential bioweapon ricin as a Category B Agent. Ricin is a so-called A/B toxin produced by plants and is one of the deadliest molecules known. It is easy to prepare and no curative treatment is available. An immunotherapeutic approach could be of interest to attenuate or neutralise the effects of the toxin. We sought to characterise neutralising monoclonal antibodies against ricin and to develop an effective therapy. For this purpose, mouse monoclonal antibodies (mAbs) were produced against the two chains of ricin toxin (RTA and RTB). Seven mAbs were selected for their capacity to neutralise the cytotoxic effects of ricin in vitro. Three of these, two anti-RTB (RB34 and RB37) and one anti-RTA (RA36), when used in combination improved neutralising capacity in vitro with an IC50 of 31 ng/ml. Passive administration of association of these three mixed mAbs (4.7 µg) protected mice from intranasal challenges with ricin (5 LD50). Among those three antibodies, anti-RTB antibodies protected mice more efficiently than the anti-RTA antibody. The combination of the three antibodies protected mice up to 7.5 hours after ricin challenge. The strong in vivo neutralising capacity of this three mAbs combination makes it potentially useful for immunotherapeutic purposes in the case of ricin poisoning or possibly for prevention