Literature detail

Glycosylation of Hemagglutinin and Neuraminidase of Influenza A Virus as Signature for Ecological Spillover and Adaptation among Influenza Reservoirs.

Paul Kim^1,2 Yo Han Jang³ Soon Bin Kwon^4,5 Chung Min Lee^6,7 Gyoonhee Han^8,9 Baik Lin Seong^10,11

Affiliations 11 institutions

Vaccine Translational Research Center, Yonsei University, 50 Yonsei-ro, Seodaemun-gu, Seoul 03722, Korea. [email protected].
Department of Integrated OMICS for Biomedical Science, College of World Class University, Yonsei University, 50 Yonsei-ro, Seodaemun-gu, Seoul 03722, Korea. [email protected].
Department of Biotechnology, College of Life Science and Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-gu, Seoul 03722, Korea. [email protected].
Department of Biotechnology, College of Life Science and Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-gu, Seoul 03722, Korea. [email protected].
Vaccine Translational Research Center, Yonsei University, 50 Yonsei-ro, Seodaemun-gu, Seoul 03722, Korea. [email protected].
Department of Biotechnology, College of Life Science and Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-gu, Seoul 03722, Korea. [email protected].
Biomedicine Pharmaceutical Group, CJ Healthcare R&D Center, CJ HealthCare, 811 Deokpyeong-ro, Majang-myeon, Icheon 17389, Korea. [email protected].
Department of Biotechnology, College of Life Science and Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-gu, Seoul 03722, Korea. [email protected].
Department of Integrated OMICS for Biomedical Science, College of World Class University, Yonsei University, 50 Yonsei-ro, Seodaemun-gu, Seoul 03722, Korea. [email protected].
Department of Biotechnology, College of Life Science and Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-gu, Seoul 03722, Korea. [email protected].
Vaccine Translational Research Center, Yonsei University, 50 Yonsei-ro, Seodaemun-gu, Seoul 03722, Korea. [email protected].

PMID 29642453 2018 Viruses eng epublish

Article

Publication summary

Glycosylation of the hemagglutinin (HA) and neuraminidase (NA) of the influenza provides crucial means for immune evasion and viral fitness in a host population. However, the time-dependent dynamics of each glycosylation sites have not been addressed. We monitored the potential N-linked glycosylation (NLG) sites of over 10,000 HA and NA of H1N1 subtype isolated from human, avian, and swine species over the past century. The results show a shift in glycosylation sites as a hallmark of 1918 and 2009 pandemics, and also for the 1976 "abortive pandemic". Co-segregation of particular glycosylation sites was identified as a characteristic of zoonotic transmission from animal reservoirs, and interestingly, of "reverse zoonosis" of human viruses into swine populations as well. After the 2009 pandemic, recent isolates accrued glycosylation at canonical sites in HA, reflecting gradual seasonal adaptation, and a novel glycosylation in NA as an independent signature for adaptation among humans. Structural predictions indicated a remarkably pleiotropic influence of glycans on multiple HA epitopes for immune evasion, without sacrificing the receptor binding of HA or the activity of NA. The results provided the rationale for establishing the ecological niche of influenza viruses among the reservoir and could be implemented for influenza surveillance and improving pandemic preparedness.

ecology evolutionary biology glycosylation hemagglutinin influenza neuraminidase reverse zoonosis Animals Disease Reservoirs Glycosylation Hemagglutinin Glycoproteins, Influenza Virus Humans Influenza A virus Influenza, Human Models, Molecular Neuraminidase Orthomyxoviridae Infections Phylogeny

Structured evidence records

Evidence records

5 total

Spillover Event 2 records

Spillover Event Extraction confidence 0.90

Key finding

The paper reports animal-to-human transmission of influenza A viruses as evidenced by glycosylation signatures linked to zoonotic movements from animals to humans.

Virus

Host

Location

Supporting text

Co-segregation of particular glycosylation sites was identified as a characteristic of zoonotic transmission from animal reservoirs, and interestingly, of 'reverse zoonosis' of human viruses into swine populations as well.

Method: sequence analysis; structural prediction
Study design: phylogenetic analysis
Transmission direction: animal-to-human

Spillover Event Extraction confidence 0.90

Key finding

The study also detects reverse zoonosis events where human influenza A viruses were transmitted into swine populations.

Virus

Host

Location

Supporting text

Method: sequence analysis; structural prediction
Study design: phylogenetic analysis
Transmission direction: human-to-animal

Cross Species Transmission 1 records

Cross Species Transmission Extraction confidence 0.90

Key finding

Distinct glycosylation site patterns of H1N1 influenza A virus HA and NA were associated with viral adaptation and cross-species transmission between avian and swine hosts.

Virus

Host

Location

Supporting text

We monitored the potential N-linked glycosylation (NLG) sites of over 10,000 HA and NA of H1N1 subtype isolated from human, avian, and swine species over the past century. Co-segregation of particular glycosylation sites was identified as a characteristic of zoonotic transmission from animal reservoirs.

Method: sequence analysis; structural prediction
Study design: phylogenetic analysis
Transmission direction: animal-to-animal

Genomic Evolution 1 records

Genomic Evolution Extraction confidence 0.90

Key finding

Phylogenetic and comparative genomic analysis of more than 10,000 H1N1 sequences revealed temporal shifts and co-segregation of HA and NA glycosylation sites linked to zoonotic and reverse zoonotic transmission between avian, swine, and human hosts.

Virus

Host

Location

Supporting text

We monitored the potential N-linked glycosylation (NLG) sites of over 10,000 HA and NA of H1N1 subtype isolated from human, avian, and swine species over the past century. The results show a shift in glycosylation sites as a hallmark of 1918 and 2009 pandemics, and also for the 1976 'abortive pandemic'. Co-segregation of particular glycosylation sites was identified as a characteristic of zoonotic transmission from animal reservoirs, and of 'reverse zoonosis' of human viruses into swine populations.

Genes or proteins: hemagglutinin (HA); neuraminidase (NA)
Analysis methods: phylogenetic analysis; comparative genomic analysis

Molecular Adaptation 1 records

Molecular Adaptation Extraction confidence 0.95

Key finding

Shifts and novel glycosylation patterns in HA and NA of H1N1 influenza A viruses correspond to host adaptation, immune evasion, and zoonotic or reverse zoonotic transmission.

Virus

Host

Location

Supporting text

Glycosylation of the hemagglutinin (HA) and neuraminidase (NA) of the influenza provides crucial means for immune evasion and viral fitness in a host population. The results show a shift in glycosylation sites as a hallmark of 1918 and 2009 pandemics, co-segregation of particular glycosylation sites as a characteristic of zoonotic transmission and reverse zoonosis, and a novel glycosylation in NA as an independent signature for adaptation among humans.

Genes or proteins: hemagglutinin (HA); neuraminidase (NA)
Mechanism types: immune_escape; transmission_fitness; host_factor_interaction; pathogenicity

Citation context

References

54 references

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Evidence overview

Evidence 5

Types 4

Virus 1

Host 3

Evidence types

Spillover Event 2 Cross Species Transmission 1 Genomic Evolution 1 Molecular Adaptation 1

Linked entities

Viruses

Hosts

Locations

Publication metadata

Journal: Viruses
Volume / Issue / Pages: 10 / 4 / -
ISSN: 1999-4915
Journal country: Switzerland
DOI: 10.3390/v10040183