Evidence map›Paper›PMID 28401928›Full record

ArticleScientific reports2017

Molecular evolutionary mechanisms driving functional diversification of α-glucosidase in Lepidoptera.

Xiaotong Li, Liangen Shi, Yanyan Zhou, Hongqing Xie, Xiangping Dai, Rongqiao Li, Yuyin Chen, Huabing Wang

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.3field-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

14 citing papers in PubMed, 23 citations in OpenAlex.

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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

8 authors at 1 institution in 1 country.

Xiaotong LiCollege of Animal Sciences, Zhejiang University, Hangzhou 310058, China.
Liangen ShiCollege of Animal Sciences, Zhejiang University, Hangzhou 310058, China.
Yanyan ZhouCollege of Animal Sciences, Zhejiang University, Hangzhou 310058, China.
Hongqing XieCollege of Animal Sciences, Zhejiang University, Hangzhou 310058, China.
Xiangping DaiCollege of Animal Sciences, Zhejiang University, Hangzhou 310058, China.
Rongqiao LiCollege of Animal Sciences, Zhejiang University, Hangzhou 310058, China.
Yuyin ChenCollege of Animal Sciences, Zhejiang University, Hangzhou 310058, China.
Huabing WangCollege of Animal Sciences, Zhejiang University, Hangzhou 310058, China.
Zhejiang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The digestive tract of lepidopteran insects is unique given its highly alkaline pH. The adaptive plasticity of digestive enzymes in this environment is crucial to the highly-efficient nutritional absorption in Lepidoptera. However, little is known about the molecular adaptation of digestive enzymes to this environment. Here, we show that lepidopteran α-glucosidase, a pivotal digestive enzyme, diverged into sucrose hydrolase (SUH) and other maltase subfamilies. SUH, which is specific for sucrose, was only detected in Lepidoptera. It suggests that lepidopteran insects have evolved an enhanced ability to hydrolyse sucrose, their major energy source. Gene duplications and exon-shuffling produced multiple copies of α-glucosidase in different microsyntenic regions. Furthermore, SUH showed significant functional divergence (FD) compared with maltase, which was affected by positive selection at specific lineages and codons. Nine sites, which were involved in both FD and positive selection, were located around the ligand-binding groove of SUH. These sites could be responsible for the ligand-binding preference and hydrolytic specificity of SUH for sucrose, and contribute to its conformational stability. Overall, our study demonstrated that positive selection is an important evolutionary force for the adaptive diversification of α-glucosidase, and for the exclusive presence of membrane-associated SUHs in the unique lepidopteran digestive tract.

Indexed as

Evolution, Molecularalpha-GlucosidasesAnimalsExonsGene DuplicationHydrolasesIntronsLepidopteraPhylogenyProtein Structure, TertiarySelection, Geneticalpha-GlucosidasesHydrolases

Identifiers

PMID28401928
PMCPMC5388851
OpenAlexW2607044911

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.