Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Lectins and Toxins.

Ke-Yi Wang1, Qiang Xu

  • 1Shanghai Institute of Biochemistry, the Chinese Academy of Sciences, Shanghai 200031, China. kyw0717@sunm.shcnc.ac.cn

Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao Acta Biochimica Et Biophysica Sinica
|June 21, 2002
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Reconstruction strategies for extensive bone defects following resection of primary malignant tumors in the distal radius.

Frontiers in oncology·2025
Same author

Feasibility and Outcomes of Vessel-Sparing Surgery for Soft Tissue Sarcoma of the Thigh Adjacent to Femoral Vessels.

Therapeutics and clinical risk management·2025
Same author

High-throughput untargeted metabolomic profiling of urinary biomarkers in acute myocarditis patients: a cross-sectional study.

Scientific reports·2025
Same author

Effect of probiotics and paraprobiotics on patients with sleep disorders and sub-healthy sleep conditions: a meta-analysis of randomized controlled trials.

Frontiers in neurology·2024
Same author

New records and revised distribution of tiger beetles in China (Coleoptera, Cicindelidae).

ZooKeys·2024
Same author

Mazabraud's syndrome in female patients: Two case reports.

World journal of orthopedics·2024
Same journal

[Prokaryotic expression and characterization of rice Rac protein osRACB].

Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica·2003
Same journal

[Purification of a big defensin from Ruditapes philippinesis and its antibacterial activity].

Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica·2003
Same journal

[Expression, purification and identification of recombinant SARS coronavirus membrane protein].

Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica·2003
Same journal

[Molecular cloning of mTSARG3 gene related to apoptosis in mouse spermatogenic cells].

Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica·2003
Same journal

[The immunopotentiation of human B lymphocyte stimulator C-terminal peptide].

Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica·2003
Same journal

[Cloning, eukaryotic expression and function assay of recombinant leukemia inhibitory factor gene LIF].

Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica·2003
See all related articles

Lectins and toxins share similarities, with some lectins exhibiting toxin-like properties and vice-versa. This suggests both molecules may play roles in organismal defense mechanisms.

Area of Science:

  • Biochemistry
  • Toxicology
  • Molecular Biology

Background:

  • Lectins, while generally not highly toxic, exhibit relationships with certain toxins.
  • BEA-type toxins possess distinct sugar-binding and enzymatic domains, influencing their toxicity and targeting.
  • Organisms utilize diverse defense mechanisms, potentially involving both lectins and toxins.

Purpose of the Study:

  • To explore the intricate relationship between lectins and toxins.
  • To investigate the shared properties and potential functional overlaps between lectins and toxins.
  • To understand the role of lectins and toxins in the defense strategies of various organisms.

Main Methods:

  • Comparative analysis of lectin and toxin structures and functions.
  • Isolation and characterization of lectins from specific sources (e.g., Trichosanthes kirilowii, Pinellia turnata, snake venom).

Related Experiment Videos

  • Examination of amino acid sequence homology between venom components and lectins.

    • Main Results:

    • Lectins from Trichosanthes kirilowii share characteristics with BEA-type toxins like ricin.
    • Certain lectins, such as one from Pinellia turnata, may function as cell membrane-perforating agents.
    • Snake venom contains lectins homologous to other venom components, and phospholipase A(2) receptors have lectin-like domains.

    Conclusions:

    • Lectins and toxins may not be mutually exclusive categories but can share functional and structural attributes.
    • The presence of lectin-like domains in toxin receptors and homologous sequences in venom components suggests convergent evolution or shared ancestry.
    • Both lectins and toxins likely contribute to the complex defense mechanisms employed by living organisms.