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Proteinquakes in the evolution of influenza virus hemagglutinin (A/H1N1) under opposing migration and vaccination pressures.

Phillips JC - Biomed Res Int (2015)

Bottom Line: Here we show that, while HA evolution is much more complex than NA evolution, it still shows abrupt punctuation changes linked to punctuation changes of NA.HA exhibits proteinquakes, which resemble earthquakes and are related to hydropathic shifting of sialic acid binding regions.Our comprehensive results present a historical (1945-2011) panorama of HA evolution over thousands of strains and are consistent with many studies of HA and NA interactions based on a few mutations of a few strains.

View Article: PubMed Central - PubMed

Affiliation: Department of Physics and Astronomy, Rutgers University, Piscataway, NJ 08854, USA.

ABSTRACT
Influenza virus contains two highly variable envelope glycoproteins, hemagglutinin (HA) and neuraminidase (NA). Here we show that, while HA evolution is much more complex than NA evolution, it still shows abrupt punctuation changes linked to punctuation changes of NA. HA exhibits proteinquakes, which resemble earthquakes and are related to hydropathic shifting of sialic acid binding regions. HA proteinquakes based on shifting sialic acid interactions are required for optimal balance between the receptor-binding and receptor-destroying activities of HA and NA for efficient virus replication. Our comprehensive results present a historical (1945-2011) panorama of HA evolution over thousands of strains and are consistent with many studies of HA and NA interactions based on a few mutations of a few strains.

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Related in: MedlinePlus

The army vaccination punctuation W = 111 (MZ) chain profiles resemble an earthquake with respect to the sialic acid binding site 130–230 relative to its HA1 matrix (see text). Note that the main feature of the sialic acid binding site is not only the hydrophilic extrema at its end points, but also the flattening of the HA butterfly profile across the entire 130–230 binding range, especially in 1950. This reflects the strongly one-dimensional nature of network water film packages, which is not obvious in Euclidean simulations of protein dynamics using effective water models.
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fig6: The army vaccination punctuation W = 111 (MZ) chain profiles resemble an earthquake with respect to the sialic acid binding site 130–230 relative to its HA1 matrix (see text). Note that the main feature of the sialic acid binding site is not only the hydrophilic extrema at its end points, but also the flattening of the HA butterfly profile across the entire 130–230 binding range, especially in 1950. This reflects the strongly one-dimensional nature of network water film packages, which is not obvious in Euclidean simulations of protein dynamics using effective water models.

Mentions: What does this precursive pattern mean? It is mysteriously similar to an earthquake with a precursor and an aftershock, but that is not so mysterious after all (Figure 6). If proteins are indeed near self-organized critical states, then they might well exhibit tertiary hydropathic shocks resembling template earthquakes, as one of the first (and still perhaps the most popular, 640 papers) applications of SOC has been to earthquakes [15–17], where collisions of tectonic plates are described by spring-block models [18]. These quakes occur in the water film packaging HA1 and resemble earthquakes in the earth's crust. Growing actin networks also exhibit sporadic effects predicted by SOC [19]. These structural changes can be described as proteinquakes.


Proteinquakes in the evolution of influenza virus hemagglutinin (A/H1N1) under opposing migration and vaccination pressures.

Phillips JC - Biomed Res Int (2015)

The army vaccination punctuation W = 111 (MZ) chain profiles resemble an earthquake with respect to the sialic acid binding site 130–230 relative to its HA1 matrix (see text). Note that the main feature of the sialic acid binding site is not only the hydrophilic extrema at its end points, but also the flattening of the HA butterfly profile across the entire 130–230 binding range, especially in 1950. This reflects the strongly one-dimensional nature of network water film packages, which is not obvious in Euclidean simulations of protein dynamics using effective water models.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4309245&req=5

fig6: The army vaccination punctuation W = 111 (MZ) chain profiles resemble an earthquake with respect to the sialic acid binding site 130–230 relative to its HA1 matrix (see text). Note that the main feature of the sialic acid binding site is not only the hydrophilic extrema at its end points, but also the flattening of the HA butterfly profile across the entire 130–230 binding range, especially in 1950. This reflects the strongly one-dimensional nature of network water film packages, which is not obvious in Euclidean simulations of protein dynamics using effective water models.
Mentions: What does this precursive pattern mean? It is mysteriously similar to an earthquake with a precursor and an aftershock, but that is not so mysterious after all (Figure 6). If proteins are indeed near self-organized critical states, then they might well exhibit tertiary hydropathic shocks resembling template earthquakes, as one of the first (and still perhaps the most popular, 640 papers) applications of SOC has been to earthquakes [15–17], where collisions of tectonic plates are described by spring-block models [18]. These quakes occur in the water film packaging HA1 and resemble earthquakes in the earth's crust. Growing actin networks also exhibit sporadic effects predicted by SOC [19]. These structural changes can be described as proteinquakes.

Bottom Line: Here we show that, while HA evolution is much more complex than NA evolution, it still shows abrupt punctuation changes linked to punctuation changes of NA.HA exhibits proteinquakes, which resemble earthquakes and are related to hydropathic shifting of sialic acid binding regions.Our comprehensive results present a historical (1945-2011) panorama of HA evolution over thousands of strains and are consistent with many studies of HA and NA interactions based on a few mutations of a few strains.

View Article: PubMed Central - PubMed

Affiliation: Department of Physics and Astronomy, Rutgers University, Piscataway, NJ 08854, USA.

ABSTRACT
Influenza virus contains two highly variable envelope glycoproteins, hemagglutinin (HA) and neuraminidase (NA). Here we show that, while HA evolution is much more complex than NA evolution, it still shows abrupt punctuation changes linked to punctuation changes of NA. HA exhibits proteinquakes, which resemble earthquakes and are related to hydropathic shifting of sialic acid binding regions. HA proteinquakes based on shifting sialic acid interactions are required for optimal balance between the receptor-binding and receptor-destroying activities of HA and NA for efficient virus replication. Our comprehensive results present a historical (1945-2011) panorama of HA evolution over thousands of strains and are consistent with many studies of HA and NA interactions based on a few mutations of a few strains.

Show MeSH
Related in: MedlinePlus