Evidence map›Paper›PMID 33327635›Full record

ArticlePolymers2020

Antibacterial Mechanism of Silkworm Seroins.

Hongtao Zhu, Xiaolu Zhang, Mengyao Lu, Haiqin Chen, Shiyi Chen, Jiaxuan Han, Yan Zhang, Ping Zhao, Zhaoming Dong

Open access · goldAbstract read
In one paragraph

Article in Polymers, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

11 citing papers in PubMed, 34 citations in OpenAlex.

  1. Virulence · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Assessment of Healing Potential ofMedicines (Basel, Switzerland) · 2025
    Article
  8. Review
  9. Review
  10. Study of the Antioxidative Effects ofMolecules (Basel, Switzerland) · 2022
    Article
  11. 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

9 authors at 1 institution in 1 country.

Hongtao ZhuState Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China.
Xiaolu ZhangState Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China.
Mengyao LuState Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China.
Haiqin ChenState Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China.
Shiyi ChenState Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China.
Jiaxuan HanState Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China.
Yan ZhangState Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China.
Ping ZhaoState Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China.
Zhaoming DongState Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China.ORCID 0000-0001-5665-9953
Southwest University · CN

Funding

Chongqing Research Program of Basic Research and Frontier Technology cstc2017jcyjAX0177Chongqing Research Program of Basic Research and Frontier Technology cstc2019jcyj-msxmX0272Fundamental Research Funds for the Central Universities of China XDJK2020D004National Natural Science Foundation of China No. 31702184
6 · The paper itself

Abstract

Seroin 1 and seroin 2 are abundant in silkworm cocoon silk and show strong antibacterial activities, and thus are thought to protect cocoon silk from damage by bacteria. In this study, we characterized the expression pattern of silkworm seroin 3, and found that seroin 3 is synthesized in the female ovary and secreted into egg to play its roles. After being infected, seroin 1, 2, and 3 were significantly up-regulated in the silkworm. We synthesized the full-length protein of seroin 1, 2, and 3 and their N/C-terminal domain (seroin-N/C), and compared the antimicrobial activities in vitro. All three seroins showed higher antibacterial activity against Gram-positive bacteria than against Gram-negative bacteria. Seroin 2 showed better antibacterial effect than seroin 1 and 3, whereas seroin 1/2/3-N was better than seroin 1/2/3-C. We found that seroin 2-C has stronger peptidoglycan binding ability than seroin 2-N per the ELISA test. The binding sites of seroin 2 with bacteria were blocked by peptidoglycan, which resulted in the loss of the antibacterial activity of seroin 2. Collectively, these findings suggest that seroin 1 and 2 play antibacterial roles in cocoon silk, whereas seroin 3 functions in the eggs. The three silkworm seroins have the same antibacterial mechanism, that is, binding to bacterial peptidoglycan by the C-terminal domain and inhibiting bacterial growth by the N-terminal domain.

Indexed as

antibacterial proteinBombyx moriseroinsilk protein

Identifiers

PMID33327635
PMCPMC7765120
OpenAlexW3113302614

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.