Identification of hemagglutinin structural domain and polymorphisms which may modulate swine H1N1 interactions with human receptor

Veljković, Veljko; Niman, Henry L.; Glišić, Sanja; Veljković, Nevena; Perovic, Vladimir; Muller, Claude P.

doi:10.1186/1472-6807-9-62

Cited by 64 publications

(108 citation statements)

References 12 publications

(15 reference statements)

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Section: Informational Spectrum Methodsmentioning

confidence: 99%

Receptor binding specificity and sequence comparison of a novel avian-origin H7N9 virus in China

Hu¹

2013

JBiSE

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Avian influenza such as H5N1 could infect humans and cause great health concern due to its high mortality rate. In March 2013, a novel reassortant avianorigin influenza A (H7N9) virus was found in several patients with severe respiratory illness in China. Since then, at least 82 people in China have been infected with this new virus and 17 have died from this virus. The question of how these people were infected with this virus and whether this virus will spread among people remains an urgent topic for research. This study took an early investigation of this virus by comparing the collected viral genome sequences of 2013 H7N9 in China against those of previous avian H7N9 and examined the receptor binding specificity of this new virus. This virus was found to be very different from the previous avian H7N9 viruses and surprisingly many of the internal proteins of 2013 H7N9 from the avian and human hosts in China were either identical or similar. Our analysis of the HA protein of this virus implied that the current strains of 2013 H7N9 in China displayed avian type receptors as their primary binding preference and human type receptors as secondary. For pandemic risk assessment, we also detected 23 mutations, including a few well known for host adaptation, in the HA1 domain of the HA protein from this virus. Each mutation was quantified for its impact on the recaptor binding selection using a bioinformatics approach. Collectively these current mutations tended to decrease the HA binding affinity for avian type recaptors and increase that for human type receptors, which could enhance the ability of this virus to infect humans.

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Section: Informational Spectrum Methodsmentioning

confidence: 99%

Receptor binding specificity and sequence comparison of a novel avian-origin H7N9 virus in China

Hu¹

2013

JBiSE

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“…In [12,13] the same research group applied the ISM to investigate the interaction between HA and its receptors. Their findings showed that HA1 of different flu subtypes encodes one highly conserved domain that might be determinants of HA binding affinity.…”

Section: Introductionmentioning

confidence: 99%

Identification of highly conserved domains in hemagglutinin associated with the receptor binding specificity of influenza viruses: 2009 H1N1, avian H5N1, and swine H1N2

Hu¹

2010

JBiSE

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The hemagglutinin (HA) of influenza viruses facilitates receptor binding and membrane fusion, which is the initial step of virus infection. Human influenza viruses preferentially bind to receptors with α2-6 linkages to galactose (SAα2,6Gal), whereas avian influenza viruses prefer receptors with α2-3 linkages to galactose (SAα2,3Gal). The current 2009 H1N1 pandemic is caused by a novel influenza A virus that has its genetic materials from birds, humans, and pigs. Its pandemic nature is characterized clearly by its dual binding to the α2-3 as well as α2-6 receptors, because the seasonal human H1N1 virus only binds to the α2-6 receptor. In a previous study, the informational spectrum method (ISM), a bioinformatics technique, was applied to uncover one highly conserved region in the HA protein associated with receptor binding preference in each of various influenza subtypes. In the present study, we extended the previous work by discovering multiple such domains in HA of 2009 H1N1 and avian H5N1 to expand our repertoire of known key regions in HA responsible for receptor binding affinity. Three such domains in HA of 2009 H1N1 were found at residue positions 106 to 130, 150 to 174, and 191 to 221, and another three domains in HA of avian H5N1 were located at residue positions 46 to 65, 136 to 153, and 269 to 286. These identified domains could be utilized as therapeutic and diagnostic targets for the prevention and treatment of influenza infection.

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“…The ISM was successfully applied to quantify the effects of HA mutations on the receptor binding preference in [10] and reveal the change of receptor binding selection caused by the mutations identified in [28] and [12]. Table 1 shows several common IS frequencies identified in [12,13]. It was observed in [11] that some of the influenza strains displayed dual HA receptor binding preference.…”

Section: Informational Spectrum Methodsmentioning

confidence: 99%

“…According to the ISM theory, the peak frequencies of IS of a protein sequence reflect its biological or biochemical functions. The ISM was successfully applied to quantify the effects of HA mutations on the receptor binding preference in [10] and reveal the change of receptor binding selection caused by the mutations identified in [28] and [12]. Table 1 shows several common IS frequencies identified in [12,13].…”

Section: Informational Spectrum Methodsmentioning

confidence: 99%

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Characterization of asian and north American avian H5N1

2011

AJMB

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Since the emerge of the highly pathogenic avian H5N1 virus in Asia in 1996, the possibility for this virus to cross species barriers to infect humans and its ability to cause large outbreaks in birds have been a public health concern. This virus has been spreading from Asia to Europe and Africa by migratory birds with North America as its next possible stop. In this study, an ensemble of computational techniques including Random Forests, Informational Spectrum Method, Entropy, and Mutual Information were employed to unravel the distinct characteristics of Asian and North American avian H5N1 in comparison with human and swine H5N1. Critical differences were identified in the HA cleavage and binding sites, the HA receptor selection, the interaction patterns of HA and NA, and NP, PA, PB1, and PB2, and the important sites in the influenza proteins including HA, NA, M1, M2, NS1, NS2, NP, PA, PB1, PB1-F2, and PB2.

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Identification of hemagglutinin structural domain and polymorphisms which may modulate swine H1N1 interactions with human receptor

Cited by 64 publications

References 12 publications

Receptor binding specificity and sequence comparison of a novel avian-origin H7N9 virus in China

Receptor binding specificity and sequence comparison of a novel avian-origin H7N9 virus in China

Identification of highly conserved domains in hemagglutinin associated with the receptor binding specificity of influenza viruses: 2009 H1N1, avian H5N1, and swine H1N2

Characterization of asian and north American avian H5N1

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