Lyme disease, science, and society: Camp Other

Monday, September 26, 2011

1 The Curious Case Of Cholesterol

This article got passed on to me:

Scientists Disarm AIDS Virus’ Attack on Immune System
http://www.voanews.com/english/news/health/-Scientists-Disarm-AIDS-Virus-Attack-on-Immune-System-130313993.html

And you might be looking at that title, wondering what HIV has to do with Lyme disease.

Well, I'm wondering if there is any relationship...

Excerpt:

"Scientists say they have found a way to disarm the AIDS virus in research that could lead to a vaccine. Researchers have discovered that if they eliminate a cholesterol membrane surrounding the virus, HIV cannot disrupt communication among disease-fighting cells and the immune system returns to normal.

Scientists have discovered that HIV needs cholesterol, which it picks up from the first immune cells it infects, to keep the virus' outer membrane fluid. That allows it to communicate with - and disrupt - the body's immune system."

Chlamydia apparently has a membrane with cholesterol in it, as does Borrelia burgdorferi (review this entry posted on Friday). I wonder if Borrelia burgdorferi can do the same thing to the immune system that HIV does? Does it disrupt communication among disease-fighting cells, too? It certainly does evade the immune system even though the immune system gives it a huge response when present.

1 comment:

  1. Somewhat related and fascinating:

    The Ixodes scapularis salivary protein, salp15, prevents the association of HIV-1 gp120 and CD4
    Source:
    http://www.ncbi.nlm.nih.gov/pubmed/18162176

    Abstract

    Ixodes scapularis salivary protein, Salp15, inhibits CD4(+) T cell activation by binding to the most-extracellular domains of the CD4 molecule, potentially overlapping with the gp120-binding region. We now show that Salp15 inhibits the interaction of gp120 and CD4. Furthermore, Salp15 prevents syncytia formation between HL2/3 (a stable HeLa cell line expressing the envelope protein) and CD4-expressing cells. Salp15 prevented gp120-CD4 interaction at least partially through its direct interaction with the envelope glycoprotein. A phage display library screen provided the interacting residues in the C1 domain of gp120. These results provide a potential basis to define exposed gp120 epitopes for the generation of neutralizing vaccines.

    ReplyDelete

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