[net-gold] MEDICAL DISEASES AIDS HIV ACQUIRED IMMUNE DEFICIENCY : MEDICAL: RESEARCH: NIH-Led Scientists Find Antibodies that Prevent Most HIV Strains from Infecting Human Cells
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- Date: Mon, 27 Sep 2010 00:26:09 -0400 (EDT)
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MEDICAL DISEASES AIDS HIV ACQUIRED IMMUNE DEFICIENCY :
MEDICAL: RESEARCH:
NIH-Led Scientists Find Antibodies that
Prevent Most HIV Strains from Infecting Human Cells
Date: Thu, 8 Jul 2010 14:15:28 -0400
From: "NIH OLIB (NIH/OD)" <olib@xxxxxxxxxx>
To: NIHPRESS@xxxxxxxxxxxx
Subject: NIH-Led Scientists Find Antibodies that
Prevent Most HIV Strains from Infecting Human Cells
U.S. Department of Health and Human Services
NATIONAL INSTITUTES OF HEALTH NIH News
National Institute of Allergy and Infectious Diseases (NIAID)
http://www.niaid.nih.gov/
Embargoed for Release: Thursday, July 8, 2010, 2 p.m. EDT
NIH-LED SCIENTISTS FIND ANTIBODIES THAT
PREVENT MOST HIV STRAINS FROM INFECTING HUMAN CELLS
Discovery to Advance HIV Vaccine Design, Antibody Therapy for Other
Diseases
Scientists have discovered two potent human antibodies that can stop more
than 90 percent of known global HIV strains from infecting human cells in
the laboratory, and have demonstrated how one of these disease-fighting
proteins accomplishes this feat. According to the scientists, these
antibodies could be used to design improved HIV vaccines, or could be
further developed to prevent or treat HIV infection. Moreover, the method
used to find these antibodies could be applied to isolate therapeutic
antibodies for other infectious diseases as well.
"The discovery of these exceptionally broadly neutralizing antibodies to
HIV and the structural analysis that explains how they work are exciting
advances that will accelerate our efforts to find a preventive HIV vaccine
for global use," says Anthony S. Fauci, M.D., director of the National
Institute of Allergy and Infectious Diseases (NIAID), National Institutes
of Health. "In addition, the technique the teams used to find the new
antibodies represents a novel strategy that could be applied to vaccine
design for many other infectious diseases."
Led by a team from the NIAID Vaccine Research Center (VRC), the scientists
found two naturally occurring, powerful antibodies called VRC01 and VRC02
in an HIV-infected individual's blood. They found the antibodies using a
novel molecular device they developed that homes in on the specific cells
that make antibodies against HIV. The device is an HIV protein that the
scientists modified so it would react only with antibodies specific to the
site where the virus binds to cells it infects.
The scientists found that VRC01 and VRC02 neutralize more HIV strains with
greater overall strength than previously known antibodies to the virus.
The researchers also determined the atomic-level structure of VRC01 when
it is attaching to HIV. This has enabled the team to define how the
antibody works and to precisely locate where it attaches to the virus.
With this knowledge, they have begun to design components of a candidate
vaccine that could teach the human immune system to make antibodies
similar to VRC01 that might prevent infection by the vast majority of HIV
strains worldwide.
NIAID scientists Peter D. Kwong, Ph.D., John R. Mascola, M.D., and Gary J.
Nabel, M.D., Ph.D., led the two research teams. A pair of articles about
these findings appears today in the online edition of Science.
"We have used our knowledge of the structure of a virus-in this case, the
outer surface of HIV-to refine molecular tools that pinpoint the
vulnerable spot on the virus and guide us to antibodies that attach to
this spot, blocking the virus from infecting cells," explains Dr. Nabel,
the VRC director.
Finding individual antibodies that can neutralize HIV strains anywhere in
the world has been difficult because the virus continuously changes its
surface proteins to evade recognition by the immune system. As a
consequence of these changes, an enormous number of HIV variants exist
worldwide. Even so, scientists have identified a few areas on HIV's
surface that remain nearly constant across all variants. One such area,
located on the surface spikes used by HIV to attach to immune system cells
and infect them, is called the CD4 binding site. VRC01 and VRC02 block HIV
infection by attaching to the CD4 binding site, preventing the virus from
latching onto immune cells.
"The antibodies attach to a virtually unchanging part of the virus, and
this explains why they can neutralize such an extraordinary range of HIV
strains," says Dr. Mascola, the deputy director of the VRC.
With these antibodies in hand, a team led by Dr. Kwong, chief of the
structural biology section at the VRC, determined the atomic-level
molecular structure of VRC01 when attached to the CD4 binding site. They
then examined this structure in light of natural antibody development to
ascertain the steps that would be needed to elicit a VRC01-like antibody
through vaccination.
Antibody development begins with the mixing of genes into new combinations
within the immune cells that make antibodies. Examination of the structure
of VRC01 attached to HIV suggested that, from a genetic standpoint, the
immune system likely could produce VRC01 precursors readily. The
researchers also confirmed that VRC01 does not bind to human cells-a
characteristic that might otherwise lead to its elimination during immune
development, a natural mechanism the body employs to prevent autoimmune
disease.
In the final stage of antibody development, antibody-producing B cells
recognize specific parts of a pathogen and then mutate, or mature, so the
antibody can bind to the pathogen more firmly. VRC01 precursors do not
bind tightly to HIV, but rather mature extensively into more powerfully
neutralizing forms. This extensive antibody maturation presents a
challenge for vaccine design. In their paper, Dr. Kwong and colleagues
explore how this challenge might be addressed by designing vaccine
components that could guide the immune system through this stepwise
maturation process and facilitate the generation of a VRC01-like antibody
from its precursors. The scientists currently are performing research to
identify these components.
The HTML version of this release contains the image:
http://www.niaid.nih.gov/SiteCollectionImages/
topics/hivaids/VRC01CD410.jpg
"The discoveries we have made may overcome the limitations that have long
stymied antibody-based HIV vaccine design," says Dr. Kwong.
The two research teams included NIAID scientists from the VRC, the
Laboratory of Immunoregulation, and the Division of Clinical Research, all
in Bethesda, Md.; as well as researchers from Beth Israel Deaconess
Medical Center in Boston; Columbia University in New York; Harvard Medical
School and Harvard School of Public Health in Boston; The Rockefeller
University in New York City; and University of Washington in Seattle.
NIAID conducts and supports research-at NIH, throughout the United States,
and worldwide-to study the causes of infectious and immune-mediated
diseases, and to develop better means of preventing, diagnosing and
treating these illnesses. News releases, fact sheets and other
NIAID-related materials are available on the NIAID Web site at
http://www.niaid.nih.gov
The National Institutes of Health (NIH) -- The Nation's Medical Research
Agency -- includes 27 Institutes and Centers and is a component of the
U.S. Department of Health and Human Services. It is the primary federal
agency for conducting and supporting basic, clinical and translational
medical research, and it investigates the causes, treatments, and cures
for both common and rare diseases. For more information about NIH and its
programs, visit
http://www.nih.gov
----------------------------------
REFERENCES:
Wu X et al.
Rational design of envelope surface identifies broadly
neutralizing human monoclonal antibodies to HIV-1.
Science.
DOI: 10.1126/science.1187659 (2010).
Zhou T et al.
Structural basis for broad and potent neutralization of
HIV-1 by antibody VRC01.
Science.
DOI: 10.1126/science.1192819 (2010).
##
This NIH News Release is available online at:
http://www.nih.gov/news/health/jul2010/niaid-08.htm
Sincerely,
David Dillard
Temple University
(215) 204 - 4584
jwne@xxxxxxxxxx
http://daviddillard.businesscard2.com
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