Special Issue "Bacterial Toxins: Structure–Function Relationship"
Deadline for manuscript submissions: 31 May 2018
Dr. Subramanyam Swaminathan
Bacterial toxins are classified into two major types: Endotoxins and exotoxins. Endotoxins are specifically referred to as cell-associated toxins—non-protein lipopolysaccharides associated with the cell wall of Gram negative bacteria. They act at, or near, the bacterial growth site. Exotoxins are proteins secreted by bacteria and act at a site farther away from the secretion site. Enterotoxins, neurotoxins, cytotoxins, lysins (e.g., hemolysin), gangrene-producing toxins, etc., are some examples of bacterial endotoxins, the names also indicating the site of action of the toxin. Most of the exotoxins have enzymatic activity. Many bacterial toxins consist of two components, A and B subunits, and are called AB toxins. Subunit B is involved in binding to the target, a specific receptor and subunit A performs the catalytic action on a substrate. Diphtheria toxin and botulinum toxins are AB toxins which contain a translocation component in the binding subunit. Shiga and Cholera toxins are AB5 toxins indicating the presence of five binding subunits and one A subunit. Pore-forming toxins (PFT) form pores in the membrane for translocation of toxin component as in anthrax toxin and colicin or involved in ion movement disruption as in toxins. Interestingly, some toxins, such as botulinum toxins, have clinical applications.
This Special Issue will focus on exotoxins, their structures and biological function explained on the basis of their structure, the major emphasis being on structure– function relationships and counter measures to block the toxin activity. The structures of stand-alone individual protein toxins provide basic information about the fold and organization of the different components. However, their complexes with appropriate substrates and/or receptors are important since they help in both understanding the protein–protein interaction responsible for toxic activity and ways to disrupt the interaction to mitigate the effect of toxin. Recent developments in cryo-electron microscopy have made it possible to study large multi-protein complexes at near atomic resolution. This Special Issue will cover the expansive structural information available so far.
Dr. Subramanyam Swaminathan
Manuscript Submission Information
Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.
Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed open access monthly journal published by MDPI.
Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1500 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.
- bacterial toxins
- three-dimensional structure
- toxin-receptor/substrate complexes
- counter measures