Lysenin, a novel sphingomyelin-specific binding protein - PubMed (original) (raw)
Case Reports
. 1998 Feb 27;273(9):5300-6.
doi: 10.1074/jbc.273.9.5300.
Affiliations
- PMID: 9478988
- DOI: 10.1074/jbc.273.9.5300
Free article
Case Reports
Lysenin, a novel sphingomyelin-specific binding protein
A Yamaji et al. J Biol Chem. 1998.
Free article
Abstract
Lysenin, a novel 41-kDa protein purified from coelomic fluid of the earthworm Eisenia foetida, induced erythrocyte lysis. Preincubation of lysenin with vesicles containing sphingomyelin inhibited lysenin-induced hemolysis completely, whereas vesicles containing phospholipids other than sphingomyelin showed no inhibitory activity, suggesting that lysenin bound specifically to sphingomyelin on erythrocyte membranes. The specific binding of lysenin to sphingomyelin was confirmed by enzyme-linked immunosorbent assay, TLC immunostaining, and liposome lysis assay. In these assays, lysenin bound specifically to sphingomyelin and did not show any cross-reaction with other phospholipids including sphingomyelin analogs such as sphingosine, ceramide, and sphingosylphosphorylcholine, indicating that it recognized a precise molecular structure of sphingomyelin. Kinetic analysis of the lysenin-sphingomyelin interaction by surface plasmon resonance measurements using BIAcoreTM system showed that lysenin associated with membrane surfaces composed of sphingomyelin (kon = 3.2 x 10(4) M-1 s-1) and dissociated extremely slowly (koff = 1.7 x 10(-4) s-1), giving a low dissociation constant (KD = 5.3 x 10(-9) M). Incorporation of cholesterol into the sphingomyelin membrane significantly increased the total amount of lysenin bound to the membrane, whereas it did not change the kinetic parameters of the lysenin-membrane interaction, suggesting that lysenin specifically recognized sphingomyelin and cholesterol incorporation changed the topological distribution of sphingomyelin in the membranes, thereby increasing the accessibility of sphingomyelin to lysenin. Immunofluorescence staining of fibroblasts derived from a patient with Niemann-Pick disease type A showed that lysenin stained the surfaces of the fibroblasts uniformly, whereas intense lysosomal staining was observed when the cells were permeabilized by digitonin treatment. Preincubation of lysenin with vesicles containing sphingomyelin abolished lysenin immunostaining. This study demonstrated that lysenin bound specifically to sphingomyelin on cellular membranes and should be a useful tool to probe the molecular motion and function of sphingomyelin in biological membranes.
Similar articles
- Oligomerization and pore formation of a sphingomyelin-specific toxin, lysenin.
Yamaji-Hasegawa A, Makino A, Baba T, Senoh Y, Kimura-Suda H, Sato SB, Terada N, Ohno S, Kiyokawa E, Umeda M, Kobayashi T. Yamaji-Hasegawa A, et al. J Biol Chem. 2003 Jun 20;278(25):22762-70. doi: 10.1074/jbc.M213209200. Epub 2003 Apr 3. J Biol Chem. 2003. PMID: 12676961 - Cholesterol and lipid/protein ratio control the oligomerization of a sphingomyelin-specific toxin, lysenin.
Ishitsuka R, Kobayashi T. Ishitsuka R, et al. Biochemistry. 2007 Feb 13;46(6):1495-502. doi: 10.1021/bi061290k. Epub 2007 Jan 23. Biochemistry. 2007. PMID: 17243772 - Lysenin-His, a sphingomyelin-recognizing toxin, requires tryptophan 20 for cation-selective channel assembly but not for membrane binding.
Kwiatkowska K, Hordejuk R, Szymczyk P, Kulma M, Abdel-Shakor AB, Płucienniczak A, Dołowy K, Szewczyk A, Sobota A. Kwiatkowska K, et al. Mol Membr Biol. 2007 Mar-Apr;24(2):121-34. doi: 10.1080/09687860600995540. Mol Membr Biol. 2007. PMID: 17453419 - Biology of lysenin, a protein in the coelomic fluid of the earthworm Eisenia foetida.
Kobayashi H, Ohta N, Umeda M. Kobayashi H, et al. Int Rev Cytol. 2004;236:45-99. doi: 10.1016/S0074-7696(04)36002-X. Int Rev Cytol. 2004. PMID: 15261736 Review. - Earthworm-derived pore-forming toxin lysenin and screening of its inhibitors.
Sukumwang N, Umezawa K. Sukumwang N, et al. Toxins (Basel). 2013 Aug 8;5(8):1392-401. doi: 10.3390/toxins5081392. Toxins (Basel). 2013. PMID: 23965430 Free PMC article. Review.
Cited by
- Dynamic Monitoring of Time-Dependent Evolution of Biomolecules Using Quantum Dots-Based Biosensors Assemblies.
Bocu R. Bocu R. Biosensors (Basel). 2024 Aug 7;14(8):380. doi: 10.3390/bios14080380. Biosensors (Basel). 2024. PMID: 39194609 Free PMC article. - A non-toxic equinatoxin-II reveals the dynamics and distribution of sphingomyelin in the cytosolic leaflet of the plasma membrane.
Mori T, Niki T, Uchida Y, Mukai K, Kuchitsu Y, Kishimoto T, Sakai S, Makino A, Kobayashi T, Arai H, Yokota Y, Taguchi T, Suzuki KGN. Mori T, et al. Sci Rep. 2024 Jul 23;14(1):16872. doi: 10.1038/s41598-024-67803-2. Sci Rep. 2024. PMID: 39043900 Free PMC article. - Development of Genetically Encoded Fluorescent KSR1-Based Probes to Track Ceramides during Phagocytosis.
Girik V, van Ek L, Dentand Quadri I, Azam M, Cruz Cobo M, Mandavit M, Riezman I, Riezman H, Gavin AC, Nunes-Hasler P. Girik V, et al. Int J Mol Sci. 2024 Mar 5;25(5):2996. doi: 10.3390/ijms25052996. Int J Mol Sci. 2024. PMID: 38474242 Free PMC article. - Non-viral Gene Therapy for Melanoma Using Lysenin from Eisenia Foetida.
Ren M, Yang L, He L, Wang J, Zhao W, Yang C, Yang S, Cheng H, Huang M, Gou M. Ren M, et al. Adv Sci (Weinh). 2024 May;11(17):e2306076. doi: 10.1002/advs.202306076. Epub 2024 Mar 6. Adv Sci (Weinh). 2024. PMID: 38445883 Free PMC article. - HIV-1 Gag targeting to the plasma membrane reorganizes sphingomyelin-rich and cholesterol-rich lipid domains.
Tomishige N, Bin Nasim M, Murate M, Pollet B, Didier P, Godet J, Richert L, Sako Y, Mély Y, Kobayashi T. Tomishige N, et al. Nat Commun. 2023 Nov 21;14(1):7353. doi: 10.1038/s41467-023-42994-w. Nat Commun. 2023. PMID: 37990014 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources