Over the last 3 years, four of them have required liver transplantation for liver failure and portal hypertension [2,3]. Examination of the explants showed a typical aspect of nodular regenerative hyperplasia related to diffuse obliterative

portal venopathy, as shown in Figure 1. Areas of hepatoportal sclerosis (HPS) were also seen in the explants. For this reason, we prefer the term ‘HIV-associated obliterative portopathy’ (HIV-OP), which better describes the syndrome of NCPH in HIV-positive patients than do the terms HPS, nodular regenerative hyperplasia (NRH), and idiopathic portal hypertension that can be found in the literature. All of these terms refer more to the consequence than to the cause of HIV-associated

NCPH [4,5]. In view of these findings, we have Sirolimus nmr PTC124 cell line screened all of our patients for coagulation abnormalities and found, in an unexpectedly high proportion of patients, a protein S (PS) deficiency [median PS level 56% of normal (IQR 46–59)] secondary to the abnormal presence of anti-PS immunoglobulin G (IgG) neutralizing antibodies [2]. We believe that the accuracy of the use of PS (activity or antigen) to diagnose early HIV-OP should be assessed. As our data suggest a prothrombotic state, use of anticoagulants is also an important issue that should be addressed in a clinical study, as oral anticoagulants Phosphoglycerate kinase are effective in preventing thrombosis in congenital PS deficiencies.

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“A cold shock domain (CSD)-containing protein, CspD, of molecular mass ∼7.28 kDa in a psychrotolerant Antarctic Janthinobacterium sp. Ant5-2 (ATCC BAA-2154) exhibited constitutive expression at 37, 22, 15, 4 and −1 °C. The cspD gene encoding the CspD protein of Ant5-2 was cloned, sequenced and analyzed. The deduced protein sequence was highly similar to the conserved domains of the cold shock proteins (Csps) from bacteria belonging to the class Betaproteobacteria. Its expression was both time- and growth phase-dependent and increased when exposed to 37 °C and UV radiation (UVC, dose: 1.8 and 2.8 mJ cm−2). The results from the electrophoretic mobility shift and subcellular localization study confirmed its single-stranded DNA-binding property. In silico analysis of the deduced tertiary structure of CspD from Ant5-2 showed a highly stable domain-swapped dimer, forming two similar monomeric Csp folds. This study established an overall framework of the structure, function and phylogenetic analysis of CspD from an Antarctic Janthinobacterium sp. Ant5-2, which may facilitate and stimulate the study of CSD fold proteins in the class Betaproteobacteria. Microorganisms isolated from Antarctica are suitable candidates to study physiological and genetic mechanisms for the adaptation to cold and subzero temperatures.