Comments on: Influenza virus attachment to cells: role of different sialic acids

By: Avian H5N1 influenza and biosecurity on Science Friday

Avian H5N1 influenza and biosecurity on Science Friday — Fri, 06 Jan 2012 21:26:57 +0000

[...] virus to allow it to bind sialic acid receptors found in the mammalian respiratory tract. These types of modifications are widely known in the virology community and could easily be done before passaging the virus in [...]

By: Vishal Kale

Vishal Kale — Wed, 14 Dec 2011 10:27:00 +0000

where and how influenza virus strains are binding to the sialic acid attached to galactose (2,6) linkage in humans ?

By: Andrew Broadbent

Andrew Broadbent — Wed, 26 Oct 2011 23:26:00 +0000

If influenza binds to the terminal sialic acid residue at a site distant from the cell membrane, how is this “sensed” by the cell, leading to receptor-mediated endocytosis? Does binding cause a conformational change in the protein to which the sialic acid is attached?

By: Hussain, Javed

Hussain, Javed — Fri, 16 Sep 2011 09:45:00 +0000

can you plz provide me the activated structure of sialic acid and NA during the reaction.
Javed Hussain

By: profvrr

profvrr — Tue, 07 Jun 2011 17:21:00 +0000

Sialic acid is the last sugar moiety in the chain of sugars attached
to a glycoprotein.

By: Mark Borris

Mark Borris — Tue, 07 Jun 2011 17:16:00 +0000

can I ask of where sialic acid attaches to in a human skin mast cell protein?

By: Daniel Ljb

Daniel Ljb — Wed, 23 Feb 2011 16:07:00 +0000

any one have any idea about which reported strains replicate in or infects alpha-2,3 SA receptor bearing cells? how about for alpha-2,6 expressing cells?

By: Vincent_tse_hk

Vincent_tse_hk — Mon, 30 Aug 2010 22:43:19 +0000

i had kept the questions for a week long and couldnt find it out. but finally, get the answer here. I love it. Cheers~!!!

By: profvrr

profvrr — Mon, 07 Dec 2009 22:06:10 +0000

Sequences of influenza H1 antigenic sites can be found in Science.
2004 Mar 19;303(5665):1866-70. Structure of the uncleaved human H1
hemagglutinin from the extinct 1918 influenza virus.

By: profvrr

profvrr — Mon, 07 Dec 2009 22:03:19 +0000

Good question. Epithelial cells of the pig trachea have both (2,3) and
(2,6) linkages on the same cells. This has been shown by staining
sections of pig trachea with lectins (sugar-binding proteins) specific
for either (2,3) or (2,6) sialic acids. The cells react with both
lectins.

By: rasaee_mj

rasaee_mj — Mon, 07 Dec 2009 18:52:15 +0000

Can any one let me know what is the sequence of main epitops on H1 .I am preparing polyclonal antibody against this protein .

By: profvrr

profvrr — Mon, 07 Dec 2009 14:06:10 +0000

Sequences of influenza H1 antigenic sites can be found in Science.
2004 Mar 19;303(5665):1866-70. Structure of the uncleaved human H1
hemagglutinin from the extinct 1918 influenza virus.

By: profvrr

profvrr — Mon, 07 Dec 2009 14:03:19 +0000

By: rasaee_mj

rasaee_mj — Mon, 07 Dec 2009 10:52:15 +0000

Can any one let me know what is the sequence of main epitops on H1 .I am preparing polyclonal antibody against this protein .

By: The D225G change in 2009 H1N1 influenza virus is not a concern « FluTrackers

Sat, 28 Nov 2009 11:18:13 +0000

[...] acids, and influenza virus strains vary in their affinity for them. Human influenza A strains bind preferentially to sialic acids linked to galactose by an alpha(2,6) bond, while avian and equine strains prefer alpha(2,3) linked [...]

By: The D225G change in 2009 H1N1 influenza virus is not a concern

The D225G change in 2009 H1N1 influenza virus is not a concern — Wed, 25 Nov 2009 15:29:30 +0000

By: DownBoyDown

DownBoyDown — Sun, 30 Aug 2009 14:30:46 +0000

OK, I'm a little confused with the mixing issue. One type of cell has (2,3) linked, another type of cell has (2,6). Pigs have a lot of both; humans have only a few (2,3). Good so far.

But how does mixing occur unless a single cell expresses both (2,3,) and (2,6)? I can see this phenotypic mixing if a single cell is co-infected, and Gallo showed this decades ago. But merely co-infecting the whole animal doesn't make the case because the two types of virus will be internalized by two different cells.

By: Mauricio Carrillo-Tripp

Mauricio Carrillo-Tripp — Wed, 06 May 2009 16:24:06 +0000

I wanted to say that I found the series of posts describing the different aspects (structure of influenza virions and how the viral RNAs can encode one or more proteins) and steps on the virus life cycle (attachment and entry of the virion, translation of mRNA into protein, genome replication, assembly of new particles, and release of particles from the cell) incredibly helpful, specially since these can be easily translated into the general case. By the way, great illustrations (made by you?).

I'm looking forward to read the following posts on the subject!

By: dmv

dmv — Tue, 05 May 2009 22:54:12 +0000

Well, you're doing a fine job, and I hope you keep it up. Now that I've found your blog, I intend to keep it on my reader.

By: profvrr

profvrr — Tue, 05 May 2009 22:44:48 +0000

I'm glad you are enjoying virology blog. The new strain of influenza
has brought many new readers who are interested in learning about
viruses. I've been teaching virology for 30 years, but I've taught
more people in the past week than in all those years.

By: o.jeff

o.jeff — Tue, 05 May 2009 22:35:19 +0000

Professor Racaniello,

I am very much enjoying your blog. Your enthusiasm for virology is truly infectious. (Couldn't resist.)

It is amazing how much you and your fellow virologists have managed to discover about these little beasts–all to our great benefit. Thank you very much.

By: dmv

dmv — Tue, 05 May 2009 20:59:33 +0000

Relevant post on this topic over at Effect Measure: http://scienceblogs.com/effectmeasure/2008/01/b...