ArticleMarine drugs2015
Functional diversity of anti-lipopolysaccharide factor isoforms in shrimp and their characters related to antiviral activity.
Article in Marine drugs, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Mass Spectrometry-Based Peptidomics for the Discovery and Profiling of Endogenous Peptides in Crustacean Hemolymph.ACS omega · 2026Article
- The Regulatory Effect and Molecular Mechanism of the Anti-Lipopolysaccharide Factor-like Gene on the Resistance of Shrimp (Animals : an open access journal from MDPI · 2025Article
- Machine learning and genetic algorithm-guided directed evolution for the development of antimicrobial peptides.Journal of advanced research · 2025Article
- Host Defense Proteins and Peptides with Lipopolysaccharide-Binding Activity from Marine Invertebrates and Their Therapeutic Potential in Gram-Negative Sepsis.Marine drugs · 2023Review
- A novel anti-lipopolysaccharide factor from blue swimmer crab Portunus pelagicus and its cytotoxic effect on the prokaryotic expression host, E. coli on heterologous expression.Journal, genetic engineering & biotechnology · 2023Article
- Antimicrobial Spectrum of Activity and Mechanism of Action of Linear Alpha-Helical Peptides Inspired by Shrimp Anti-Lipopolysaccharide Factors.Biomolecules · 2023Article
- Computer-Aided Screening for Potential Coronavirus 3-Chymotrypsin-like Protease (3CLpro) Inhibitory Peptides from Putative Hemp Seed Trypsinized Peptidome.Molecules (Basel, Switzerland) · 2022Article
- The sORF-Encoded Peptides, ATP Synthase Subunits, Facilitate WSSV Duplication in Shrimp.Viruses · 2022Article
- Virtual Screening for SARS-CoV-2 Main Protease Inhibitory Peptides from the Putative Hydrolyzed Peptidome of Rice Bran.Antibiotics (Basel, Switzerland) · 2022Article
- Antiviral peptides from aquatic organisms: Functionality and potential inhibitory effect on SARS-CoV-2.Aquaculture (Amsterdam, Netherlands) · 2021Review
- Molecular and Functional Characterization of an Anti-lipopolysaccharide Factor Mm-ALF from Speckled Shrimp Metapenaeus monoceros.Probiotics and antimicrobial proteins · 2021Article
- A Lymphoid Organ Specific Anti-Lipopolysaccharide Factor fromMarine drugs · 2021Article
- Anti-inflammatory activities of arthropod peptides: a systematic review.The journal of venomous animals and toxins including tropical diseases · 2021Review
- Transcriptome profiling and in silico detection of the antimicrobial peptides of red king crab Paralithodes camtschaticus.Scientific reports · 2020Article
- The Immune Activity of PT-Peptide Derived from Anti-Lipopolysaccharide Factor of the Swimming CrabMarine drugs · 2019Article
- Identification of Single Nucleotide Polymorphisms Related to the Resistance Against Acute Hepatopancreatic Necrosis Disease in the Pacific White ShrimpFrontiers in genetics · 2019Article
- Characterization of a Lymphoid Organ Specific Anti-lipopolysaccharide Factor From Shrimp Reveals Structure-Activity Relationship of the LPS-Binding Domain.Frontiers in immunology · 2019Article
- The Two NF-κB Pathways Regulating Bacterial and WSSV Infection of Shrimp.Frontiers in immunology · 2019Review
- Article
- Multiple Isoforms of Anti-Lipopolysaccharide Factors and Their Antimicrobial Functions in the Ridgetail PrawnMarine drugs · 2018Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Anti-lipopolysaccharide factor (ALF) is a small protein with broad-spectrum antimicrobial activity, which has potential application in the disease control. Previously, we isolated seven ALF isoforms from the Chinese shrimp Fenneropenaeus chinensis. In the present study, their distributions in tissues of shrimp were analyzed and the data showed that different isoforms had different expression profiles, which suggested that they might have different functions. Then, the functions of different isoforms were studied by analyzing the antibacterial and antiviral activities of the functional domain of ALFs, the LPS-binding domain (LBD), which were synthesized by chemical methods. Different ALFs showed distinct antibacterial and antiviral activities, which were consistent with their diverse tissue distribution patterns. Sequence analysis on the LBD domain of different isoforms revealed that an identical lysine residue site was specifically conserved in peptides with anti-WSSV activity. In order to confirm whether this lysine residue is critical to the antiviral activity of the peptide, new peptides were synthesized by changing residues at this site. Changing the lysine residue at the specific site to other amino acid residue, the antiviral activity of the peptide apparently decreased. While replacing other residue with a lysine residue at this site in LBD peptide without anti-WSSV activity, the peptide will obtain the antiviral activity to WSSV. These results not only showed us a comprehensive understanding on the function of ALFs from F. chinensis, but also provided clues for the development of ALFs as potential therapeutic drugs to WSSV.
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