The Administrative core will be responsible for the overall management of this HIVRAD. This Core will be responsible for interacting with DAIDS Program Officer and Staff as required by the funding mechanism as a multi-project cooperative agreement between our team and the NIH. The Core will coordinate all aspects of routine program management on administrative, financial, and regulator issues. The Administrative Core will also organize and interact with external advisors, and host annual external reviews. This Core has the following four Specific Aims: 1- To coordinate the interactions a) among scientists from different institutions included in the current program and b) between our team and Scientific Advisory Board members and NIH personnel regarding efficient implementation of the proposed plans and projects. 2- To oversee budgetary matters, including review and approval of subcontractual agreements, monitoring of monthly expenses and preparation of various reports. 3- To develop an Intellectual Property plan and provide logistical support for intellectual property filings and negotiations 4- To coordinate publications and presentations of results arising from these studies.

Public Health Relevance

This program involves scientists working at 4 different locations throughout the US and 2 sites in South Africa. For this program to operate efficiently and productively, a centralized Administrative oversight is essential. This will be provided by Dr. Pinter and his assistants, who will be responsible for coordinating communication between the participating scientists, NIH Program Officials, and internal and external Scientific Advisory Committees, and will facilitate other scientific, legal and logistical issues that may arise

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Program Projects (P01)
Project #
5P01AI088610-06
Application #
8720672
Study Section
Special Emphasis Panel (ZAI1-RB-A)
Project Start
Project End
Budget Start
2014-03-01
Budget End
2015-02-28
Support Year
6
Fiscal Year
2014
Total Cost
$195,072
Indirect Cost
$40,099
Name
Rutgers University
Department
Type
DUNS #
078795851
City
Newark
State
NJ
Country
United States
Zip Code
07103
Wibmer, Constantinos Kurt; Moore, Penny L; Morris, Lynn (2015) HIV broadly neutralizing antibody targets. Curr Opin HIV AIDS 10:135-43
Moore, Penny L; Williamson, Carolyn; Morris, Lynn (2015) Virological features associated with the development of broadly neutralizing antibodies to HIV-1. Trends Microbiol 23:204-11
Sheward, Daniel J; Ntale, Roman; Garrett, Nigel J et al. (2015) HIV-1 Superinfection Resembles Primary Infection. J Infect Dis 212:904-8
Derdeyn, Cynthia A; Moore, Penny L; Morris, Lynn (2014) Development of broadly neutralizing antibodies from autologous neutralizing antibody responses in HIV infection. Curr Opin HIV AIDS 9:210-6
Salomon, Aidy; Krachmarov, Chavdar; Lai, Zhong et al. (2014) Specific sequences commonly found in the V3 domain of HIV-1 subtype C isolates affect the overall conformation of native Env and induce a neutralization-resistant phenotype independent of V1/V2 masking. Virology 448:363-74
Wibmer, Constantinos Kurt; Bhiman, Jinal N; Gray, Elin S et al. (2013) Viral escape from HIV-1 neutralizing antibodies drives increased plasma neutralization breadth through sequential recognition of multiple epitopes and immunotypes. PLoS Pathog 9:e1003738
Sethi, Anurag; Tian, Jianhui; Derdeyn, Cynthia A et al. (2013) A mechanistic understanding of allosteric immune escape pathways in the HIV-1 envelope glycoprotein. PLoS Comput Biol 9:e1003046
Murphy, Megan K; Yue, Ling; Pan, Ruimin et al. (2013) Viral escape from neutralizing antibodies in early subtype A HIV-1 infection drives an increase in autologous neutralization breadth. PLoS Pathog 9:e1003173
Moore, Penny L; Sheward, Daniel; Nonyane, Molati et al. (2013) Multiple pathways of escape from HIV broadly cross-neutralizing V2-dependent antibodies. J Virol 87:4882-94
Moore, Penny L; Gray, Elin S; Wibmer, C Kurt et al. (2012) Evolution of an HIV glycan-dependent broadly neutralizing antibody epitope through immune escape. Nat Med 18:1688-92

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