
Talita Cristina Dellariva
State University of Campinas, São Paulo, Brazil
Title: IMPROVEMENT AND APPLICATION OF NESTED-PCR TECHNIQUE USING CONSENSUS-DEGENERATE PRIMERS TO DETECT HUMAN HERPESVIRUS IN PLASMA SAMPLES FROM HEMATOPOIETIC STEM CELL TRANSPLANTATION (HSCT) PATIENTS.
Biography
Talita Cristina Dellariva completed her degree in Biological Sciences from State University of Campinas (UNICAMP) in 2013 and nowadays she has been developing her master's degree in Clinical Medicine in the Faculty of Medical Sciences, State University of Campinas, São Paulo, Brazil.
Abstract
Human Herpesviruses (HHVs) are an important cause of infections in transplantation and immunocompromised patients in general. This group of virus consists in three subfamilies: α-herpesvirinae, β–herpesvirinae and γ–herpesvirinae which are included the eight Human Herpesviruses species. Currently, the diagnosis of infectious diseases have been a considerable advance after molecular techniques implantation, especially the Polymerase Chain Reation (PCR), once it presents high sensitivity and specificity to detect low quantities of nucleic acids. The use of consensus-degenerate primers in PCR has been used as an efficient alternative for the detection and identification of Herpesviridae family members in clinical samples. The aim of this study was to improve the Nested-PCR (N-PCR) technique using consensus-degenerate primers to detect human herpesvirus subfamilies. Forty plasma-DNA samples from HSCT patients were analyzed using N-PCR technique with degenerate primers in both reactions. These primers were designed from highly conserved amino acid sequences of herpesviral DNA polymerase gene. The results show that 8/40 (20%) were positive to α-herpesvirinae and/or γ–herpesvirinae; 19/40 (47.5%) were positive to β–herpesvirinae and 5/40 (12.5%) presented coinfection with the three subfamilies. The development and improvement of N-PCR using consensus-degenerate primers have been fundamentally important in helping the clinical diagnosis, therapy, classification and epidemiological studies of viruses and to discover new herpesvirus species.

Marcin Skorenski
Wroclaw University of Technology,Poland
Title: Design and synthesis of selective, irreversible inhibitors of HAT protease- promising drug target for influenza treatment.
Biography
Marcin Skoreński is PhD student at Wroclaw University of Technology, Faculty of Chemistry, Division of Medicinal Chemistry and Microbiology. His research is focused on the development of low molecular weight compounds designed to target proteases involved in the pathogenesis of v viral infections (hepatitis C virus (HCV)n West Nile virus (WNV), herpes viruses, influenza). He is a co-author of 5papers, 14 patents and more than 10 pending patent applications.
Abstract
The HAT protease also known as TMPRSS11D or airway trypsin-like protease is a member of the serine protease family. In humans HAT is responsible for several biologically important processes including modulation of urokinase-type plasminogen activator receptor and fibrinogen processing. Moreover elevated level of HAT has been reported for patients suffering from chronic skin diseases (such as psoriasis) and respiratory tract dysfunction. Additionaly HAT was found to cleave the surface glycoprotein hemagglutinin of the influenza virus. Without this proces virus particles can not enter the host cel and start replication procesc, thus enzyme responsible for this cleavage are consider as promising drug target for influenza treatment. The main objective of our research was the design and synthesis of selective, irreversible, active site-directed inhibitors of HAT protease. The target compounds belong to the group of phosphonic analogues of amino acids containing various, structurally diverse ester groups. These compounds are known as highly specific and irreversible inhibitors of serine proteases and have been successfully used as inhibitors of many physiologically important serine proteases such as thrombin, human neutrophil elastase, cathepsin G, proteinase 3, and dipeptidyl peptidase IV. Since the complete biological and physiological functions of HAT protease are yet to be discovered, the development of potent and specific inhibitors might provide very useful tools to study the HAT. Some recent reports consider HAT protease as a promising therapeutic target which inactivation could potentially limit the influenza virus infection hence the development of specific inhibitors might lead to a new class of antiviral agents.