Evidence map›Paper›PMID 11090165›Full record

ArticleJournal of virology2000

A functional NSP4 enterotoxin peptide secreted from rotavirus-infected cells.

M Zhang, C Q Zeng, A P Morris, M K Estes

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

60 citing papers in PubMed, 168 citations in OpenAlex.

  1. Secreted Nonstructural Protein 3 is a Pathogenic Determinant of Orbivirus.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
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  14. Foal Diarrhea: Established and Postulated Causes, Prevention, Diagnostics, and Treatments.The Veterinary clinics of North America. Equine practice · 2018
    Review
  15. Review
  16. Article
  17. Rotavirus NSP4Virus genes · 2017
    Article
  18. Article
  19. Article
  20. The effect of bovine rotavirus and its nonstructural protein 4 on ER stress-mediated apoptosis in HeLa and HT-29 cells.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
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

4 authors at 2 institutions in 1 country.

M ZhangDivision of Molecular Virology, Baylor College of Medicine, University of Texas Health Science Center, Houston, Texas 77030, USA.
C Q Zeng
A P Morris
M K Estes
Baylor College of Medicine · USThe University of Texas Health Science Center at Houston · US

Funding

MOLECULAR BIOLOGY OF THE ROTAVIRUSESR01DK030144 · NIDDK · BAYLOR COLLEGE OF MEDICINE · PI ESTES, MARY KOLB · 1986 to 2005
$2.2M
Molecular Biology of the RotavirusesR56DK030144 · NIDDK · BAYLOR COLLEGE OF MEDICINE · PI ESTES, MARY KOLB · 2006 to 2007
$443k
NIDDK NIH HHS DK30144NIDDK NIH HHS R01 DK030144NIDDK NIH HHS R56 DK030144
6 · The paper itself

Abstract

Previous studies have shown that the nonstructural glycoprotein NSP4 plays a role in rotavirus pathogenesis by functioning as an enterotoxin. One prediction of the mechanism of action of this enterotoxin was that it is secreted from virus-infected cells. In this study, the media of cultured (i) insect cells infected with a recombinant baculovirus expressing NSP4, (ii) monkey kidney (MA104) cells infected with the simian (SA11) or porcine attenuated (OSU-a) rotavirus, and (iii) human intestinal (HT29) cells infected with SA11 were examined to determine if NSP4 was detectable. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis-Western blotting, immunoprecipitation and N-terminal amino acid sequencing identified, in the early media from virus-infected cells, a secreted, cleavage product of NSP4 with an apparent molecular weight of 7,000 that represented amino acids 112 to 175 (NSP4 aa112-175). The secretion of NSP4 aa112-175 was not affected by treatment of cells with brefeldin A but was abolished by treatment with nocodazole and cytochalasin D, indicating that secretion of this protein occurs via a nonclassical, Golgi apparatus-independent mechanism that utilizes the microtubule and actin microfilament network. A partial gene fragment coding for NSP4 aa112-175 was cloned and expressed using the baculovirus-insect cell system. Purified NSP4 aa112-175 increased intracellular calcium mobilization in intestinal cells when added exogenously, and in insect cells when expressed endogenously, similarly to full-length NSP4. NSP4 aa112-175 caused diarrhea in neonatal mice, as did full-length NSP4. These results indicate that NSP4 aa112-175 is a functional NSP4 enterotoxin peptide secreted from rotavirus-infected cells.

Indexed as

AnimalsCell LineGlycoproteinsHaplorhiniHumansMiceReceptors, VirusRotavirusRotavirus InfectionsSwineToxins, BiologicalViral Nonstructural ProteinsVirus ReplicationGlycoproteinsNS28 protein, rotavirusReceptors, VirusToxins, BiologicalViral Nonstructural Proteins

Identifiers

PMID11090165
PMCPMC112448
OpenAlexW1989038840

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.