Evidence map›Paper›PMID 20881037›Full record

ArticleJournal of virology2010

Impairment of hepatitis B virus virion secretion by single-amino-acid substitutions in the small envelope protein and rescue by a novel glycosylation site.

Kiyoaki Ito, Yanli Qin, Michael Guarnieri, Tamako Garcia, Karen Kwei, Masashi Mizokami, Jiming Zhang, Jisu Li, Jack R Wands, Shuping Tong

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

64 citing papers in PubMed, 108 citations in OpenAlex.

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4 more citing papers are in PubMed but not listed here.

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

10 authors at 4 institutions in 3 countries.

Kiyoaki ItoLiver Research Center, Rhode Island Hospital, Warren Alpert School of Medicine, Brown University, Providence, Rhode Island 02906, USA.
Yanli Qin
Michael Guarnieri
Tamako Garcia
Karen Kwei
Masashi Mizokami
Jiming Zhang
Jisu Li
Jack R Wands
Shuping Tong
Brown University · USRhode Island Hospital · USHuashan Hospital · CNNational Center for Global Health and Medicine · JP

Funding

STUDY OF HBV AND/OR VARIANTS IN ALCOHOLICSR01AA008169 · NIAAA · RHODE ISLAND HOSPITAL (PROVIDENCE, RI) · PI WANDS, JACK R · 1989 to 2011
$3.9M
Biomarker for Hepatocellular CarcinomaR01CA123544 · NCI · RHODE ISLAND HOSPITAL · PI WANDS, JACK R · 2007 to 2011
$1.2M
Molecular Target(s) for Interruption of HBV InfectionR01CA109733 · NCI · RHODE ISLAND HOSPITAL · PI LI, JISU · 2005 to 2009
$1.1M
NCI NIH HHS CA109733NCI NIH HHS CA123544NCI NIH HHS R01 CA109733NCI NIH HHS R01 CA123544NIAAA NIH HHS AA08169NIAAA NIH HHS R01 AA008169
6 · The paper itself

Abstract

Mutations in the S region of the hepatitis B virus (HBV) envelope gene are associated with immune escape, occult infection, and resistance to therapy. We previously identified naturally occurring mutations in the S gene that alter HBV virion secretion. Here we used transcomplementation assay to confirm that the I110M, G119E, and R169P mutations in the S domain of viral envelope proteins impair virion secretion and that an M133T mutation rescues virion secretion of the I110M and G119E mutants. The G119E mutation impaired detection of secreted hepatitis B surface antigen (HBsAg), suggesting immune escape. The R169P mutant protein is defective in HBsAg secretion as well and has a dominant negative effect when it is coexpressed with wild-type envelope proteins. Although the S domain is present in all three envelope proteins, the I110M, G119E, and R169P mutations impair virion secretion through the small envelope protein. Conversely, coexpression of just the small envelope protein of the M133T mutant could rescue virion secretion. The M133T mutation could also overcome the secretion defect caused by the G145R immune-escape mutation or mutation at N146, the site of N-linked glycosylation. In fact, the M133T mutation creates a novel N-linked glycosylation site ((131)NST(133)). Destroying this site by N131Q/T mutation or preventing glycosylation by tunicamycin treatment of transfected cells abrogated the effect of the M133T mutation. Our findings demonstrate that N-linked glycosylation of HBV envelope proteins is critical for virion secretion and that the secretion defect caused by mutations in the S protein can be rescued by an extra glycosylation site.

Indexed as

Virus ReplicationAlkaline PhosphataseAmino Acid SubstitutionBlotting, WesternDNA ReplicationGenotypeGlycosylationHepatitis BHepatitis B Surface AntigensHepatitis B virusHumansMutagenesis, Site-DirectedMutationPhenotypeProtein PrecursorsViral Envelope ProteinsAlkaline PhosphataseHepatitis B Surface Antigenspresurface protein 1, hepatitis B surface antigenProtein PrecursorsViral Envelope Proteins

Identifiers

PMID20881037
PMCPMC3004315
OpenAlexW2135323216

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.