Bundlin A
* Please be kindly noted products are not for therapeutic use. We do not sell to patients.
| Category | Antibiotics |
| Catalog number | BBF-00188 |
| CAS | 23623-31-6 |
| Molecular Weight | 459.53 |
| Molecular Formula | C25H33NO7 |
Online Inquiry
Description
Bundlin A is a macrolide antibiotic produced by Streptomyces greseofuscus. It has antimicrobial activity against individual gram-positive bacteria such as Staphylococcus aureus and individual fungi such as Daoxizi.
Specification
| Synonyms | Lankacidin C; Antibiotic T-2636 C |
| IUPAC Name | N-[(1S,2R,3E,5E,7S,9E,11E,13S,15R,19R)-7,13-dihydroxy-1,4,10,19-tetramethyl-17,18-dioxo-16-oxabicyclo[13.2.2]nonadeca-3,5,9,11-tetraen-2-yl]-2-oxopropanamide |
| Canonical SMILES | CC1C2CC(C=CC(=CCC(C=CC(=CC(C(C1=O)(C(=O)O2)C)NC(=O)C(=O)C)C)O)C)O |
| InChI | InChI=1S/C25H33NO7/c1-14-6-9-18(28)10-8-15(2)12-21(26-23(31)17(4)27)25(5)22(30)16(3)20(33-24(25)32)13-19(29)11-7-14/h6-8,10-12,16,18-21,28-29H,9,13H2,1-5H3,(H,26,31)/b10-8+,11-7+,14-6+,15-12+/t16-,18+,19-,20-,21-,25+/m1/s1 |
| InChI Key | ATDILMLBOZKFGI-JUTMVFGESA-N |
Properties
| Appearance | Needle Crystal |
| Antibiotic Activity Spectrum | Gram-positive bacteria; Fungi |
| Melting Point | 205-207°C |
| Density | 1.23 g/cm3 |
Reference Reading
1. N-acetyllactosamine-induced retraction of bundle-forming pili regulates virulence-associated gene expression in enteropathogenic Escherichia coli
Romney M Humphries, Thomas P Griener, Stefanie L Vogt, George L Mulvey, Tracy Raivio, Michael S Donnenberg, Pavel I Kitov, Michael Surette, Glen D Armstrong Mol Microbiol. 2010 Jun 1;76(5):1111-26. doi: 10.1111/j.1365-2958.2010.07192.x. Epub 2010 May 4.
Enteropathogenic Escherichia coli (EPEC) are a major cause of infant morbidity and mortality due to diarrhoea in developing countries. The pathogenesis of EPEC is dependent on a coordinated multi-step process culminating in the intimate adherence of the organisms to the host's intestinal mucosa. During the initial stages of the EPEC colonization process, the fimbrial adhesin, bundle-forming pili (BFP), plays an integral role. We previously reported that the major BFP structural subunit, bundlin, displays lectin-like properties, which enables BFP to initially tether EPEC to N-acetyllactosamine (LacNAc) glycan receptors on host cell surfaces. We also reported that incubating EPEC with synthetic LacNAc-bearing neoglycoconjugates not only inhibits their adherence to host cells, but also induces BFP retraction and subsequent degradation of the bundlin subunits. Herein, we demonstrate that the periplasmic serine protease, DegP, is required for degrading bundlin during this process. We also show that DegP appears to act as a bundlin chaperone during BFP assembly and that LacNAc-BSA-induced BFP retraction is followed by transcriptional upregulation of the BFP operon and downregulation of the locus of enterocyte effacement operons in EPEC.
2. Interactions of enteropathogenic Escherichia coli with pediatric and adult intestinal biopsy specimens during early adherence
Romney M Humphries, Christopher C M Waterhouse, George Mulvey, Paul Beck, Glen D Armstrong Infect Immun. 2009 Oct;77(10):4463-8. doi: 10.1128/IAI.00686-09. Epub 2009 Jul 27.
Enteropathogenic Escherichia coli (EPEC) strains cause watery diarrhea almost exclusively in young children. The basis for this age discrimination has never been determined, but it may be related to host cell receptors. During infection, EPEC strains express type IV bundle-forming pili composed of repeating subunits of the protein called bundlin. The very first interaction between EPEC and in vitro-cultured epithelial cells is mediated by the binding of alpha-bundlin to a carbohydrate receptor that contains, at a minimum, the N-acetyllactosamine (LacNAc) glycan sequence. However, bundlins expressed from the beta-bundlin allele do not bind LacNAc glycan sequences. Herein, we investigated whether EPEC strains use alpha-bundlin to mediate early adherence to human intestinal biopsy specimens cultured in vitro by assessing the ability of isogenic EPEC mutants expressing either the alpha(1)- or beta(1)-bundlin allele or a bundlin-deficient EPEC strain to bind to these specimens. Furthermore, we directly compared the abilities of a wild-type EPEC strain to bind to the epithelial surfaces of both human adult and pediatric biopsy specimens. Our results demonstrate that beta-bundlin does not act as an adhesin during early EPEC adherence to adult duodenal biopsy specimens. The results also indicate that EPEC binds equally well to adult and pediatric biopsy specimens in an early adherence assay. This result is supported by the finding that the early adherence of EPEC to both adult and pediatric biopsy specimens was inhibited by LacNAc neoglycoconjugates, suggesting that organisms expressing alpha-bundlin-type bundle-forming pili initially bind to related glycan receptors in both age groups.
3. From alpha to beta: identification of amino acids required for the N-acetyllactosamine-specific lectin-like activity of bundlin
Romney M Humphries, Michael S Donnenberg, Jonathan Strecker, Elena Kitova, John S Klassen, Lina Cui, Thomas P Griener, George L Mulvey, Glen D Armstrong Mol Microbiol. 2009 May;72(4):859-68. doi: 10.1111/j.1365-2958.2009.06679.x. Epub 2009 Apr 14.
Bundle-forming pili (BFP) promote the adherence of typical enteropathogenic Escherichia coli (EPEC) to human intestinal epithelial cells. BFP are polymers of bundlin and nine bundlin alleles have been identified in EPEC isolated from diverse sources. These alleles are divided into two main groups, alpha and beta, based on their amino acid sequences. Alpha bundlins are also N-acetyllactosamine- (LacNAc) specific lectins and bind to HEp-2 cells, whereas beta bundlins do not display these characteristics. The four surface-exposed regions of amino acid sequence heterogeneity between alpha and beta bundlin were therefore investigated as potential LacNAc-specific carbohydrate-binding domains in a bundlin. Mutation of one of these domains, 137-GENNI-141, in alpha(1) bundlin to that of beta bundlin (136-SPDST-140) resulted in BFP that no longer bound to LacNAc or HEp-2 cells. Conversely, mutating the beta3 bundlin gene to encode the alpha bundlin sequence at this domain resulted in the gain of HEp-2 cell adherence. The importance of this domain in carbohydrate binding is supported by the finding that introducing the mutation GENNI-->GENNT altered the alpha1 bundlin carbohydrate-binding specificity from LacNAc to the Lewis X glycan sequence.
Recommended Products
| BBF-02642 | Lactonamycin | Inquiry |
| BBF-02614 | Nystatin | Inquiry |
| BBF-00677 | 3-Amino-3-deoxy-D-glucose | Inquiry |
| BBF-03754 | CASTANOSPERMINE | Inquiry |
| BBF-00764 | Cerebroside C | Inquiry |
| BBF-03753 | Baicalin | Inquiry |
Bio Calculators
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
* Total Molecular Weight:
g/mol
Tip: Chemical formula is case sensitive. C22H30N4O √ c22h30n40 ╳
