Evidence map›Paper›PMID 27493644›Full record

ArticleFrontiers in microbiology2016

The New Antimicrobial Peptide SpHyastatin from the Mud Crab Scylla paramamosain with Multiple Antimicrobial Mechanisms and High Effect on Bacterial Infection.

Zhongguo Shan, Kexin Zhu, Hui Peng, Bei Chen, Jie Liu, Fangyi Chen, Xiaowan Ma, Shuping Wang, Kun Qiao, Kejian Wang

Abstract read
In one paragraph

Article in Frontiers in microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

  1. Review
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  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. A truncated peptide SpgillcinFrontiers in cellular and infection microbiology · 2022
    Article
  13. Article
  14. A Novel Antimicrobial Peptide Sparanegtin Identified inInternational journal of molecular sciences · 2021
    Article
  15. Review
  16. A Novel Antimicrobial Peptide SparamosinFrontiers in microbiology · 2021
    Article
  17. The Long-Term Effect of a Nine Amino-Acid Antimicrobial Peptide AS-hepc3Frontiers in cellular and infection microbiology · 2021
    Article
  18. Article
  19. Antimicrobial Mechanism of pBD2 againstMolecules (Basel, Switzerland) · 2020
    Article
  20. Enhanced Immune Protection of Mud CrabFrontiers in immunology · 2020
    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

10 authors.

Zhongguo ShanState Key Laboratory of Marine Environmental Science, College of Ocean & Earth Science, Xiamen University Xiamen, China.
Kexin ZhuState Key Laboratory of Marine Environmental Science, College of Ocean & Earth Science, Xiamen University Xiamen, China.
Hui PengState Key Laboratory of Marine Environmental Science, College of Ocean & Earth Science, Xiamen UniversityXiamen, China; Fujian Collaborative Innovation Center for Exploitation and Utilization of Marine Biological Resources, Xiamen UniversityXiamen, China; State-Province Joint Engineering Laboratory of Marine Bioproducts and Technology, Xiamen UniversityXiamen, China.
Bei ChenState Key Laboratory of Marine Environmental Science, College of Ocean & Earth Science, Xiamen University Xiamen, China.
Jie LiuState Key Laboratory of Marine Environmental Science, College of Ocean & Earth Science, Xiamen University Xiamen, China.
Fangyi ChenState Key Laboratory of Marine Environmental Science, College of Ocean & Earth Science, Xiamen UniversityXiamen, China; Fujian Collaborative Innovation Center for Exploitation and Utilization of Marine Biological Resources, Xiamen UniversityXiamen, China; State-Province Joint Engineering Laboratory of Marine Bioproducts and Technology, Xiamen UniversityXiamen, China.
Xiaowan MaState Key Laboratory of Marine Environmental Science, College of Ocean & Earth Science, Xiamen University Xiamen, China.
Shuping WangState Key Laboratory of Marine Environmental Science, College of Ocean & Earth Science, Xiamen University Xiamen, China.
Kun QiaoState Key Laboratory of Marine Environmental Science, College of Ocean & Earth Science, Xiamen University Xiamen, China.
Kejian WangState Key Laboratory of Marine Environmental Science, College of Ocean & Earth Science, Xiamen UniversityXiamen, China; Fujian Collaborative Innovation Center for Exploitation and Utilization of Marine Biological Resources, Xiamen UniversityXiamen, China; State-Province Joint Engineering Laboratory of Marine Bioproducts and Technology, Xiamen UniversityXiamen, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SpHyastatin was first identified as a new cationic antimicrobial peptide in hemocytes of the mud crab Scylla paramamosain. Based on the amino acid sequences deduced, it was predicted that this peptide was composed of two different functional domains, a proline-rich domain (PRD) and a cysteine-rich domain (CRD). The recombinant product of SpHyastatin displayed potent antimicrobial activities against the human pathogen Staphylococcus aureus and the aquatic animal pathogens Aeromonas hydrophila and Pseudomonas fluorescens. Compared with the CRD of SpHyastatin, the PRD presented better antimicrobial and chitin binding activities, but both regions were essential for allowing SpHyastatin complete antimicrobial activity. The binding properties of SpHyastatin to different microbial surface molecules suggested that this might be an initial and crucial step for performing its antimicrobial activities. Evaluated using propidium iodide uptake assays and scanning electron microscopy images, the antimicrobial mechanism of SpHyastatin was found to be prone to disrupt cell membrane integrity. Interestingly, SpHyastatin exerted its role specifically on the surface of S. aureus and Pichia pastoris whereas it directly killed P. fluorescens through simultaneous targeting the membrane and the cytoplasm, indicating that SpHyastatin could use different antimicrobial mechanisms to kill different species of microbes. As expected, the recombinant SpHyastatin increased the survival rate of crabs challenged with Vibrio parahaemolyticus. In addition, SpHyastatin could modulate some V. parahaemolyticus-responsive genes in S. paramamosain.

Indexed as

antimicrobial mechanismantimicrobial peptideimmune protectionmembrane permeabilizationScylla paramamosainSpHyastatin

Identifiers

PMID27493644
PMCPMC4954822

What OpenQuestion holds

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Registered trials

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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.