Evidence map›Paper›PMID 27929750›Full record

ArticleHuman vaccines & immunotherapeutics2017

Purification and immunogenicity of hemagglutinin from highly pathogenic avian influenza virus H5N1 expressed in Nicotiana benthamiana.

Teen-Lee Pua, Xiao Ying Chan, Hwei-San Loh, Abdul Rahman Omar, Vidadi Yusibov, Konstantin Musiychuk, Alexandra C Hall, Megan V Coffin, Yoko Shoji, Jessica A Chichester and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Human vaccines & immunotherapeutics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
2.7field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 3 institutions in 2 countries.

Teen-Lee Puaa School of Biosciences, Faculty of Science, The University of Nottingham Malaysia Campus , Selangor , Malaysia.
Xiao Ying Chana School of Biosciences, Faculty of Science, The University of Nottingham Malaysia Campus , Selangor , Malaysia.
Hwei-San Loha School of Biosciences, Faculty of Science, The University of Nottingham Malaysia Campus , Selangor , Malaysia.
Abdul Rahman Omarc Institute of Bioscience, Universiti Putra Malaysia , Selangor , Malaysia.
Vidadi Yusibovd Fraunhofer USA Center for Molecular Biotechnology , Newark , DE , USA.
Konstantin Musiychukd Fraunhofer USA Center for Molecular Biotechnology , Newark , DE , USA.
Alexandra C Halld Fraunhofer USA Center for Molecular Biotechnology , Newark , DE , USA.
Megan V Coffind Fraunhofer USA Center for Molecular Biotechnology , Newark , DE , USA.
Yoko Shojid Fraunhofer USA Center for Molecular Biotechnology , Newark , DE , USA.
Jessica A Chichesterd Fraunhofer USA Center for Molecular Biotechnology , Newark , DE , USA.
Hong Bid Fraunhofer USA Center for Molecular Biotechnology , Newark , DE , USA.
Stephen J Streatfieldd Fraunhofer USA Center for Molecular Biotechnology , Newark , DE , USA.
Fraunhofer USA Center for Molecular Biotechnology · USUniversity of Nottingham Malaysia Campus · MYUniversiti Putra Malaysia · MY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Highly pathogenic avian influenza (HPAI) H5N1 is an ongoing global health concern due to its severe sporadic outbreaks in Asia, Africa and Europe, which poses a potential pandemic threat. The development of safe and cost-effective vaccine candidates for HPAI is considered the best strategy for managing the disease and addressing the pandemic preparedness. The most potential vaccine candidate is the antigenic determinant of influenza A virus, hemagglutinin (HA). The present research was aimed at developing optimized expression in Nicotiana benthamiana and protein purification process for HA from the Malaysian isolate of H5N1 as a vaccine antigen for HPAI H5N1. Expression of HA from the Malaysian isolate of HPAI in N. benthamiana was confirmed, and more soluble protein was expressed as truncated HA, the HA1 domain over the entire ectodomain of HA. Two different purification processes were evaluated for efficiency in terms of purity and yield. Due to the reduced yield, protein degradation and length of the 3-column purification process, the 2-column method was chosen for target purification. Purified HA1 was found immunogenic in mice inducing H5 HA-specific IgG and a hemagglutination inhibition antibody. This paper offers an alternative production system of a vaccine candidate against a locally circulating HPAI, which has a regional significance.

Indexed as

AnimalsAntibodies, ViralDisease Models, AnimalFemaleGene ExpressionHemagglutinin Glycoproteins, Influenza VirusImmunoglobulin GInfluenza A Virus, H5N1 SubtypeInfluenza VaccinesMice, Inbred BALB CNicotianaOrthomyxoviridae InfectionsRecombinant ProteinsTreatment OutcomeVaccines, SubunitVaccines, SyntheticAntibodies, Viralhemagglutinin, avian influenza A virusHemagglutinin Glycoproteins, Influenza VirusImmunoglobulin GInfluenza VaccinesRecombinant ProteinsVaccines, SubunitVaccines, Syntheticavian influenzaH5N1hemagglutininplant virus-based expression systempurificationrecombinant protein

Identifiers

PMID27929750
PMCPMC5328219
OpenAlexW2560258876

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.