The hepatitis C virus (HCV) is a positive strand RNA virus of the Flavivirus family that replicates in the cytoplasm of infected hepatocytes. Previously, several nuclear localization signals (NLS) and nuclear export signals (NES) have been identified in HCV proteins, however, there is little evidence that these proteins travel into the nucleus during infection. We have recently shown that nuclear pore complex (NPC) proteins (termed nucleoporins or Nups) are present in the membranous web and are required during HCV infection. In this study, we identify a total of 11 NLS and NES sequences in various HCV proteins. We show direct interactions between HCV proteins and importin α5 (IPOA5/kapα1), importin β3 (IPO5/kap β3), and exportin 1 (XPO1/CRM1) both in-vitro and in cell culture. These interactions can be disrupted using peptides containing the specific NLS or NES sequences of HCV proteins. Moreover, using a synchronized infection system, we show that these peptides inhibit HCV infection during distinct phases of the HCV life cycle. The inhibitory effects of these peptides place them in two groups. The first group binds IPOA5 and inhibits infection during the replication stage of HCV life cycle. The second group binds IPO5 and is active during both early replication and early assembly. This work delineates the entire life cycle of HCV and the active involvement of NLS sequences during HCV replication and assembly. Given the abundance of NLS sequences within HCV proteins, our previous finding that Nups play a role in HCV infection, and the relocation of the NLS double-GFP reporter in HCV infected cells, this work supports our previous hypothesis that NPC-like structures and nuclear transport factors function in the membranous web to create an environment conducive to viral replication.

No abstract

A few times a week, I receive e-mails inviting me to submit my manuscript to open access journals with topics ranging from software engineering to biotechnology. I have no background or expertise in these areas, but I always assumed that I received these messages because I am the contact for all of my library's journal subscriptions. After becoming familiar with the work of Jeffrey Beall, who has been working to raise awareness of what he has termed "predatory" open access publishers, I learned that that might be another, less benign explanation. Beall, scholarly initiatives librarian at the University of Colorado Denver, researches open access publishers and keeps a list of those he believes exhibit predatory behavior on his blog, Scholarly Open Access (http://scholarlyoa.com). He says these publishers exploit the gold open access model-which requires the author of an accepted article to pay a processing fee for publicationsimply to make a profit. Essentially, these publishers and journals operate as vanity presses, offering to publish nearly any article, as long as the author can pay the fee. They may also exhibit other questionable practices, such as concealing their true location and contact information or failing to properly carry out the peer review process (Elliott, 2012). Beall has published a full list of the criteria he uses to identify predatory publishers on his blog. One trademark behavior is the use of mass e-mails to solicit manuscripts, editorships, or peer reviewers (Beall, 2012). I pulled up some of my own spam and used Beall's list to check out the

No abstract

This preconference workshop aimed to teach participants the skills needed to create a technical services culture that is strategic, iterative, and innovative. The presenters drew on their experiences with agile software development to introduce attendees to the foundations of an agile organization, including project planning, project management, and workflow analysis. The workshop included a mix of instruction and hands-on activities designed to encourage reflection and application of the content.