Abstract

In Cellular and Molecular Mechanisms of Toxin Action—Pore-Forming Peptides and Protein Toxins, edited by Gianfranco Menestra, Mauro Dalla Serra, Phillip Lazarovici, the past and current state of knowledge of certain selected pore-forming protein toxins and peptides are reviewed. The book successfully describes the past and recent work on these protein and peptide pore-forming toxins. The 59 different contributors to this book summarized past work and demonstrated how current technologies have been used to better characterize these toxins and the nature of the pores they produce in cell membranes.
The text includes brief introductory and extensive advanced subject material. Throughout the book, tables, figures, and illustrations are appropriately introduced, helpful, and of good quality. The book includes several color plates that are useful in visualizing primary, secondary, tertiary, and quaternary protein structures. The book contains a glossary and a list of abbreviations that are helpful in defining many of the terms used in the text. The book also has a brief description of each of the contributors, many of which are well respected for their scientific accomplishments. Because several contributors wrote each book chapter, the writing style does vary considerably from chapter to chapter. Overall, the text is well organized and contains extensive discussions of past and recent experimental data. It successfully describes many of the current technologies used in determining how these toxins cause pores in the cell membrane. Several chapters discuss the intracellular effects of these pore-forming toxins on cellular physiology.
A weakness in the text is the differing writing styles of the various authors. Some chapters are very clear and concise, whereas others are excessively verbose, contain terms unique to the field without definition, and are lacking in clarity. There are also a significant number of misspelt words and typographical errors in this text. However, none of the errors change the meaning of the book’s content. This is not a text for the novice in the field; however, it should be appropriate for basic and industrial science researchers, postdoctoral fellows, and for advanced graduate students.
The book is organized into two parts: Part 1, Pore-Forming Proteins, and Part 2, Pore-Forming Peptides. The chapters in Part 1 describe the staphylococcal leukotoxins, RTX toxins, pseudomonal cytotoxin, vacuolating toxin of Helicobacter pylori, delta-endotoxin of Bacillus thuringiensis, colicins, and actinoporins produced by sea anemones. Although each chapter is organized somewhat differently, all of the chapters in this part of the book describe the toxin(s), the nature of the pore formed, the mechanisms of pore formation, and the toxin’s effects on the host. Each chapter contains extensive references and frequently refers the reader to recent review articles for further reading. The contributors of most of these chapters assume the reader already has significant knowledge about pore-forming proteins. Reading the preface of this text is important for a novice to properly appreciate this part the text. The introductory material is relatively short. Discussions of pore formation, measurement of pore formation in membranes and the nature of the pores formed by each protein are extensive. The contributors frequently bring the reader to the edge of the knowledge envelope in their particular topic and are not afraid to include conflicting and sometimes confusing views. This treatment of the subject matter encourages the reader to wonder what particular experiments could be designed to help us know more about these toxins and the pores they form.
Part 2 of the text (Pore-Forming Peptides) begins with an introductory chapter titled “Structural and Charge Requirements for Antimicrobial Peptide Insertion into Biological and Model Membranes.” The authors of this chapter do an excellent job of discussing the importance of many of these peptides in protecting the producer of the peptide from attack by other organisms. They discuss the presence of these peptides in a wide variety of organisms from insects to humans. They also discuss the biophysical parameters and proposed models of pore formation by these peptides. There are, however, a significant number of misspelt words in this chapter that can be a bit troublesome at times but does not affect the readers’ ability to understand the material presented.
Subsequent chapters proceed to discuss, in greater detail, the paradaxins from the Moses Sole fish, cecropinmelittin hybrid peptides, pseudomonal syringomycins and syringopeptins, and amyloid peptide channels. The authors of each of these chapters assume the reader has read the introductory chapter prior to reading their chapter. The authors of each of these chapters describe the peptide(s), the nature of the pore formed, the mechanisms of pore formation, and the toxin’s effects, if any, on the host. Each chapter also contains extensive references and frequently refers the reader to other review articles for further reading.
The last chapter of this part of the book is out of place in that the authors are discussing proteins rather than peptides. It is also the most controversial chapter. The authors of this chapter titled “The Role of Amyloid Peptide Channels in Amyloid Disease” propose that aggregation of various proteins result in channel formation of the host cells, resulting in various changes in cellular physiology that result in cell death. Much of their discussion is based on previous studies; however, many would doubt their conclusions. It is, nonetheless, stimulating to think about and might be something upon which one could further investigate.
In summary, the text is a collection of critical documents in the field that contains enough discussions of historical experimental data to give the knowledgeable reader an excellent sense of the complexities of these toxins. It further describes many of the current technologies used in determining the mechanisms of how these toxins cause pores in the cell membrane. This book is well suited for those familiar with the field and makes an excellent reference text.
