Ebola virus (EBOV) is the causative agent of a severe hemorrhagic fever disease associated with high mortality rates in humans. This virus has five strains of which Zaire Ebola virus (ZEBOV) is the first and most important strain. It can be transmitted through contact with contaminated surfaces and objects. The genome of EBOV codes one non-structural and seven structural proteins consisting of two forms of glycoprotein (GP): soluble glycoprotein (sGP) and GP (spike). In this paper, we attempted to characterize and predict physicochemical properties, B-cell epitopes, mutation sites, phosphorylation sites, glycosylation sites, and different protein structures of EBOV GP to provide comprehensive data about changes of this GP during a 40-years course (1976–2015). GP sequences were obtained from NCBI gene bank from 1976–2015. Expasy’sProtParam, PROTSCALE, immuneepitope, Bepipred, BcePred, ABCpred, VaxiJen, DISPHOS, NetPhos, and numerous programs were used to predict and analyze all sequences. More variety of mutations were found in 2015 sequences and mutations were related to huge changes in B-cell epitopes, phosphorylation and glycosylation sites. In addition, our results determined different sites of disulfide bonds and an important mutation related to IgE epitope as well as four potent B-cell epitopes (380–387, 318–338, 405–438 and 434–475). In this study, we suggested the effect of mutations on GP properties, six positions for disulfide bonds and four phosphorylation sites for protein kinase C enzyme. Selected sequences were shown different sites for O-link and N-link glycosylation. A mutation that changed GP to an allergen protein and has a significant role in vaccine designing as well as four potent B-cell epitopes in GP protein were found.

Acute respiratory infections (ARIs) in children younger than 5 years of age are one of the leading causes of morbidity and mortality, particularly in developing countries. Mycoplasma pneumoniae and Chlamydophila pneumoniae are prevalent causative agents of ARIs, worldwide. We sought M. pneumoniae and C. pneumoniae in respiratory samples from Iranian children with ARIs.  From November 2014 to April 2015, respiratory samples of 150 children aged 1 month to 15 years old were screened for presence of M. pneumoniae and C. pneumoniae. Polymerase chain reaction (PCR) and culture methods were used to detect these bacteria in respiratory samples in the form of throat swabs and nasopharyngeal aspirates. A questionnaire containing demographic and clinical information has been filled up for all participants in this study. Our obtained data showed that out of 150 tested samples, 7 (4.7%) were PCR positive for M. pneumoniae and only one (0.7%) positive sample for C. pneumoniae was detected. However, none of the tested samples was detected M. pneumoniae using the bacterial culture method. All patients with ARIs due to M. pneumoniae showed up with sore throat and flu like symptoms. According to our data, PCR method is more sensitive than culture for detection of M. pneumoniae. With regards to our results, it appears that M. pneumoniae and especially C. pneumoniae were infrequent causative agents in our studied population.

Background NS5A and NS5B proteins of hepatitis C virus (HCV) are the main targets of compounds that directly inhibit HCV infections. However, the emergence of resistance-associated substitutions (RASs) may cause substantial reductions in susceptibility to inhibitors. Methods Viral load and genotyping were determined in eighty-seven naïve HCV-infected patients, and the amplified NS5A and NS5B regions were sequenced by Sanger sequencing. In addition, physicochemical properties, structural features, immune epitopes, and inhibitors-protein interactions of sequences were analyzed using several bioinformatics tools. Results Several amino acid residue changes were found in NS5A and NS5B proteins; however, we did not find any mutations related to resistance to the treatment in NS5B. Different phosphorylation and few glycosylation sites were assessed. Disulfide bonds were identified in both proteins that had a significant effect on the function and structure of HCV proteins. Applying reliable software to predict B-cell epitopes, 3 and 5 regions were found for NS5A and NS5B, respectively, representing a considerable potential to induce the humoral immune system. Docking analysis determined amino acids involved in the interaction of inhibitors and mentioned proteins may not decrease the drug efficiency. Conclusions Strong interactions between inhibitors, NS5A and NS5B proteins and the lack of efficient drug resistance mutations in the analyzed sequences may confirm the remarkable ability of NS5A and NS5B inhibitors to control HCV infection amongst Iranian patients. The results of bioinformatics analysis could unveil all features of both proteins, which can be beneficial for further investigations on HCV drug resistance and designing novel vaccines.

No abstract

No abstract