Evidence map›Paper›PMID 11559807›Full record

ArticleJournal of virology2001

Molecular determinants of species specificity in the coronavirus receptor aminopeptidase N (CD13): influence of N-linked glycosylation.

D E Wentworth, K V Holmes

Open access · greenAbstract readComparative Study
In one paragraph

Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed, 1 pooled it
2.1field-weighted citation impact, top 13% 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

75 citing papers in PubMed, 1 synthesis or guideline pooled it, 115 citations in OpenAlex.

  1. Pooled it
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  12. Batteryless wireless magnetostrictive FeSensors and actuators. A, Physical · 2023
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15 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

2 authors at 1 institution in 1 country.

D E WentworthDepartment of Microbiology, University of Colorado Health Sciences Center, Denver, Colorado 80262, USA. Dave.Wentworth@UCHSC.edu
K V Holmes
University of Colorado Health · US

Funding

University of Colorado Cancer Center Support Grant - Lung Cancer Patient-Derived Xenografts with Autologous Human Immune SystemsP30CA046934 · NCI · UNIVERSITY OF COLORADO DENVER · PI James V Degregori · 1988 to 2026
$117.0M
NEUROVIROLOGY-MOLECULAR BIOLOGYT32NS007321 · NINDS · UNIVERSITY OF COLORADO DENVER · PI GILDEN, DONALD · 1988 to 2014
$2.3M
CORONAVIRUS-RECEPTOR INTERACTIONSR01AI026075 · NIAID · UNIVERSITY OF COLORADO DENVER · PI HOLMES, KATHRYN V · 1999 to 2003
$1.3M
CORONAVIRUS/RECEPTOR INTERACTIONSU01AI026075 · NIAID · UNIVERSITY OF COLORADO DENVER · PI HOLMES, KATHRYN V · 1988 to 1999
–
NCI NIH HHS 2 P30 CA 46934-09NCI NIH HHS CA46934NCI NIH HHS P30 CA046934NIAID NIH HHS AI26075NIAID NIH HHS R01 AI026075NINDS NIH HHS T32 NS007321NINDS NIH HHS T32 NS07321
6 · The paper itself

Abstract

Aminopeptidase N (APN), a 150-kDa metalloprotease also called CD13, serves as a receptor for serologically related coronaviruses of humans (human coronavirus 229E [HCoV-229E]), pigs, and cats. These virus-receptor interactions can be highly species specific; for example, the human coronavirus can use human APN (hAPN) but not porcine APN (pAPN) as its cellular receptor, and porcine coronaviruses can use pAPN but not hAPN. Substitution of pAPN amino acids 283 to 290 into hAPN for the corresponding amino acids 288 to 295 introduced an N-glycosylation sequon at amino acids 291 to 293 that blocked HCoV-229E receptor activity of hAPN. Substitution of two amino acids that inserted an N-glycosylation site at amino acid 291 also resulted in a mutant hAPN that lacked receptor activity because it failed to bind HCoV-229E. Single amino acid revertants that removed this sequon at amino acids 291 to 293 but had one or five pAPN amino acid substitution(s) in this region all regained HCoV-229E binding and receptor activities. To determine if other N-linked glycosylation differences between hAPN, feline APN (fAPN), and pAPN account for receptor specificity of pig and cat coronaviruses, a mutant hAPN protein that, like fAPN and pAPN, lacked a glycosylation sequon at 818 to 820 was studied. This sequon is within the region that determines receptor activity for porcine and feline coronaviruses. Mutant hAPN lacking the sequon at amino acids 818 to 820 maintained HCoV-229E receptor activity but did not gain receptor activity for porcine or feline coronaviruses. Thus, certain differences in glycosylation between coronavirus receptors from different species are critical determinants in the species specificity of infection.

Indexed as

Coronavirus 229E, HumanAmino Acid SequenceAmino Acid SubstitutionAnimalsBinding SitesCD13 AntigensCell LineCoronavirusCoronavirus, FelineCoronavirus InfectionsGlycosylationHumansMembrane GlycoproteinsMolecular Sequence DataReceptors, CoronavirusReceptors, VirusCD13 AntigensMembrane GlycoproteinsReceptors, CoronavirusReceptors, Virus

Identifiers

PMID11559807
PMCPMC114546
OpenAlexW2138641910

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.