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Microbial lectins and agglutinins. Properties and biological activity
ANALYTICAL BIOCHEMISTRY 160,240-242
(1987)
BOOK Current puter
REVIEWS
Communications in Molecular Biology: ComGraphics and Molecular Modeling. Edited by
ROBERT FLETTERICK AND MARK ZOLLER, Cold Spring Harbor, New York, 1986. 145 pp. $29. Publication of the proceedings of meetings and conferences has always been a source of dispute among the scientific literati. Cold Spring Harbor has opened an entirely new area for argument with their introduction of a series containing “extended abstracts” of papers already presented at their symposia. This volume summarizes a meeting, held in December 1985, to discuss the use of computer graphics and molecular modeling in the investigation of the structures of proteins. 1 do not think that they could have chosen a worse topic with which to introduce this new concept in journalism, The book contains 19 abstracts, ranging from two to eight medium octave pages in length. Some are illustrated and all are referenced. However, the reader is asked not to use these abstracts as literature sources. The first five discuss computer software and hardware used by a number of laboratories in this field. As usual in any high-tech field, the authors seem more interested in describing what they have rather than what they can do with it. Next come five offerings on structural principles in protein structure. Topics include the detection of sequence homologies and their use in the prediction of secondary structure in uncrystallized proteins, starting from a known structure. Briinden discusses the anatomy of cu/j3proteins, Eisenberg elaborates on the role of hydrophobic moments in the stabilization of structure, and
Microbial logical
Lectins Activity.
and Agglutinins.
Properties
the Richardsons report the latest progress in their attempts to chemically synthesize a protein of predetermined structure. Six abstracts on protein modeling show some overlap with the previous section. Greer and Jones both use known substructures as a basis for molecular model building and Taylor describes the use of supersecondary structure templates derived from X-ray structures to complement well-known statistical methods for the prediction of secondary structures from amino acid sequences. Three papers on the use of computer graphics in the determination of crystal structures and the investigation of the interactions between molecules complete this section. The final three abstracts describe the work of Karplus, Levitt, and Hagler on the molecular dynamics of protein molecules. An appendix lists around 150 institutions involved in molecular graphics work. Hardware, software, display systems, and persons to contact are listed. The last section demonstrates most clearly the limitations of the printed page as a vehicle for the presentation of this kind of work. The main appeal of molecular graphics lies in the use of color and motion. A one-page summary of a 9-min movie on protein molecular dynamics failed to yield any useful information, even though I have sat mesmerized through two earlier versions of this film. In general, I have great difficulty imagining to whom this book is directed. Its contents are too short to be of use to a newcomer to this field, but not detailed or novel enough for those who are already involved.
biotic interactions in establishing biological ecosystems, is the subject of this book. Assembled and edited by David Mirelman, this volume is composed of 20 chapters that were contributed by some of the leading research groups in the field. The following is a sampling of the chapters in order to illustrate the diversity of the contents. In Chapter 1, an overview of and orientation to our present knowledge (with literature up to and including 1984) of bacterial lectins and agglutinins is presented (D. Mirelman and I. Ofek). Chapter 2 provides information about viruses as hemagglutinins as well as an account of the by now historic role of the “receptor destroying enzyme” (M. A. K.
and Bio-
Edited by DAVID MIRELMAN, Wiley, New York, 1986. 443 pp. $57.50.
Only a few years ago, most attention on lectins was focused exclusively on their occurrence in plants. The ubiquitous occurrences of lectins and agglutinins in bacteria, protozoa, fungi, molds, and viruses are documented in this book and illustrate the importance of carbohydrate-mediated adherence to cell surfaces in many biological systems. The role that lectins and agglutinins play in “cellular recognition” processes, as well as in the pathogenicity of microorganisms or their sym-
0003-2697187 $3.00 Copyright 0 1987 by Academic Press, Inc. All rights of reproduction in any form reserved.
PETER MC PHIE
240
BOOK REVIEWS
241
the organism is presented in Chapter 9. Despite the fact Markwell). A common feature of the next chapters (3-8) is the description of microbial lectins associated with the that this is probably one of the best characterized bactefine filamentous appendages that are referred to as fim- rial lectins, its biological function remains a mystery briae (L. “fringe”) or pili (L. “hairs”). Fimbriae are stra- (D. R. Zusman, M. G. Cumsky, D. R. Nelson, and J. M. tegically located so as to be involved in the adhesive Romeo). The symbiotic association of nitrogen fixing bacteria, and their interaction with other bacteria and properties of microorganisms. plant surfaces, as well as the involvement of fimbriae in In Chapter 4, there is information about the interaction between host glycolipids and Escherichia coli lectins this process, are presented in Chapter 11 (F. B. Dazzo. resulting in urinary tract infections. Various methods J. W. Kijne, K. Haahtela, and T. K. Korhonen). The that are used to study these interactions are discussed (H. study of the pathogenic protozoan Entamoeba histolyLeffler and C. Svanorg-Eden). This is followed by a pre- tica which is known to invade the human colonic musentation of the genetic aspects of E. co/i lectins and cosa is presented in Chapter 16. Two lectins with differpossible mechanisms for evading host immune response ent carbohydrate specificity are implicated in the adherby antigenic diversity and phase variation (Chapter 5, S. ence process (D. Mirelman and J. I. Ravdin). The book is highly recommended for those in the bioNormark, M. Baga, M. Goransson, F. P. Lindberg. B. logical and medical sciences with an interest in the develLund, M. Norgen, and B. E. Uhlin). A detailed structural analysis of gonococcal pili is provided in Chapter 6. A opment of new strategies for antimicrobial agents and/or pilus receptor in host tissues remains elusive (G. K. the prevention of disease due to microorganisms. The Schoolnik, J. B. Rothbard, and E. C. Gotschlich). An contents will prove useful in the stimulation and planinteresting contribution concerns the fimbrial lectins of ning of future experimental approaches to mechanisms Actinomyces spp. that are important microbial compo- of bacterial adhesion. nents of the ecosystem in the human oral cavity (Chapter 8, J. 0. Cisar). A discussion of the mycobacterial hemagglutinin and OTHMAR GABRIEL its appearance during various developmental stages of
Vols. 114 and I 15, Diffraction Macromolecules. Edited by H.
Methods in Enzymology, Methods for Biological
W.
WYCKOFF,
C.
H.
W.
HIRS,
AND
S. N.
TI-
Academic Press, New York, 1985. Vol. 114, $64.00; Vol. 115. $55.00. MASHEFF
This two-volume addition to Methods in Enzymology signals that protein crystallography has become an essential part of modern biochemistry. The editors’ goals have been to give biochemists an introduction to the field of macromolecular structure determination by X-ray diffraction, and to give crystallographers a comprehensive summary of techniques available to them. The first volume deals with the experimental aspects from crystal growth to X-ray data measurement. The second describes the analysis of these data. methods of phase determination, and refinement of the resulting structure, with a final section on the presentation and analysis of the structure. Because of the highly technical nature of this subject, browsing biochemists will not find too much here that is readily comprehensible, although there are a few chapters, such as Max Perutz’s fascinating description of the early days of protein crystallography, that are universally interesting. The suspicion with which protein crystallographers were regarded by their small molecule contemporaries would have made Perutz today an unlikely candidate for an NIH grant, and it is a tribute to the wisdom of the British Medical Research Council that
they nurtured this infant science until it could prove itself. Perutz also makes an important point that is just as relevant today when he disposes of the legend that the structures of hemoglobin and myoglobin were solved with primitive instruments in a hut near the Cavendish Laboratory. In fact they used the best and newest equipment that was available, including one of the world’s first electronic computers. For the crystallographer, however, this will become an essential handbook, not because it contains anything particularly new, but because, in the spirit of the Methods series, it contains everything in one place. Everything is here from crystallization to instructions on how to prepare drawings of a protein structure that can be understood by medical students. In fact, some exercise of editorial restraint might have shortened the text somewhat, although some of the museum articles make most enjoyable reading. Some other aspects of the editing are more annoying, in particular the rather large number of spelling errors. Examples such as Lease Squares and Duck University, together with the existence of several versions of some authors’ names in the index mar an otherwise most valuable text. Nevertheless, these two volumes will provide the essence of what every protein crystallographer needs, at least until the next major technical advance occurs, when it will become time for the next volume. DAVID R. DAVIES
(1987)
BOOK Current puter
REVIEWS
Communications in Molecular Biology: ComGraphics and Molecular Modeling. Edited by
ROBERT FLETTERICK AND MARK ZOLLER, Cold Spring Harbor, New York, 1986. 145 pp. $29. Publication of the proceedings of meetings and conferences has always been a source of dispute among the scientific literati. Cold Spring Harbor has opened an entirely new area for argument with their introduction of a series containing “extended abstracts” of papers already presented at their symposia. This volume summarizes a meeting, held in December 1985, to discuss the use of computer graphics and molecular modeling in the investigation of the structures of proteins. 1 do not think that they could have chosen a worse topic with which to introduce this new concept in journalism, The book contains 19 abstracts, ranging from two to eight medium octave pages in length. Some are illustrated and all are referenced. However, the reader is asked not to use these abstracts as literature sources. The first five discuss computer software and hardware used by a number of laboratories in this field. As usual in any high-tech field, the authors seem more interested in describing what they have rather than what they can do with it. Next come five offerings on structural principles in protein structure. Topics include the detection of sequence homologies and their use in the prediction of secondary structure in uncrystallized proteins, starting from a known structure. Briinden discusses the anatomy of cu/j3proteins, Eisenberg elaborates on the role of hydrophobic moments in the stabilization of structure, and
Microbial logical
Lectins Activity.
and Agglutinins.
Properties
the Richardsons report the latest progress in their attempts to chemically synthesize a protein of predetermined structure. Six abstracts on protein modeling show some overlap with the previous section. Greer and Jones both use known substructures as a basis for molecular model building and Taylor describes the use of supersecondary structure templates derived from X-ray structures to complement well-known statistical methods for the prediction of secondary structures from amino acid sequences. Three papers on the use of computer graphics in the determination of crystal structures and the investigation of the interactions between molecules complete this section. The final three abstracts describe the work of Karplus, Levitt, and Hagler on the molecular dynamics of protein molecules. An appendix lists around 150 institutions involved in molecular graphics work. Hardware, software, display systems, and persons to contact are listed. The last section demonstrates most clearly the limitations of the printed page as a vehicle for the presentation of this kind of work. The main appeal of molecular graphics lies in the use of color and motion. A one-page summary of a 9-min movie on protein molecular dynamics failed to yield any useful information, even though I have sat mesmerized through two earlier versions of this film. In general, I have great difficulty imagining to whom this book is directed. Its contents are too short to be of use to a newcomer to this field, but not detailed or novel enough for those who are already involved.
biotic interactions in establishing biological ecosystems, is the subject of this book. Assembled and edited by David Mirelman, this volume is composed of 20 chapters that were contributed by some of the leading research groups in the field. The following is a sampling of the chapters in order to illustrate the diversity of the contents. In Chapter 1, an overview of and orientation to our present knowledge (with literature up to and including 1984) of bacterial lectins and agglutinins is presented (D. Mirelman and I. Ofek). Chapter 2 provides information about viruses as hemagglutinins as well as an account of the by now historic role of the “receptor destroying enzyme” (M. A. K.
and Bio-
Edited by DAVID MIRELMAN, Wiley, New York, 1986. 443 pp. $57.50.
Only a few years ago, most attention on lectins was focused exclusively on their occurrence in plants. The ubiquitous occurrences of lectins and agglutinins in bacteria, protozoa, fungi, molds, and viruses are documented in this book and illustrate the importance of carbohydrate-mediated adherence to cell surfaces in many biological systems. The role that lectins and agglutinins play in “cellular recognition” processes, as well as in the pathogenicity of microorganisms or their sym-
0003-2697187 $3.00 Copyright 0 1987 by Academic Press, Inc. All rights of reproduction in any form reserved.
PETER MC PHIE
240
BOOK REVIEWS
241
the organism is presented in Chapter 9. Despite the fact Markwell). A common feature of the next chapters (3-8) is the description of microbial lectins associated with the that this is probably one of the best characterized bactefine filamentous appendages that are referred to as fim- rial lectins, its biological function remains a mystery briae (L. “fringe”) or pili (L. “hairs”). Fimbriae are stra- (D. R. Zusman, M. G. Cumsky, D. R. Nelson, and J. M. tegically located so as to be involved in the adhesive Romeo). The symbiotic association of nitrogen fixing bacteria, and their interaction with other bacteria and properties of microorganisms. plant surfaces, as well as the involvement of fimbriae in In Chapter 4, there is information about the interaction between host glycolipids and Escherichia coli lectins this process, are presented in Chapter 11 (F. B. Dazzo. resulting in urinary tract infections. Various methods J. W. Kijne, K. Haahtela, and T. K. Korhonen). The that are used to study these interactions are discussed (H. study of the pathogenic protozoan Entamoeba histolyLeffler and C. Svanorg-Eden). This is followed by a pre- tica which is known to invade the human colonic musentation of the genetic aspects of E. co/i lectins and cosa is presented in Chapter 16. Two lectins with differpossible mechanisms for evading host immune response ent carbohydrate specificity are implicated in the adherby antigenic diversity and phase variation (Chapter 5, S. ence process (D. Mirelman and J. I. Ravdin). The book is highly recommended for those in the bioNormark, M. Baga, M. Goransson, F. P. Lindberg. B. logical and medical sciences with an interest in the develLund, M. Norgen, and B. E. Uhlin). A detailed structural analysis of gonococcal pili is provided in Chapter 6. A opment of new strategies for antimicrobial agents and/or pilus receptor in host tissues remains elusive (G. K. the prevention of disease due to microorganisms. The Schoolnik, J. B. Rothbard, and E. C. Gotschlich). An contents will prove useful in the stimulation and planinteresting contribution concerns the fimbrial lectins of ning of future experimental approaches to mechanisms Actinomyces spp. that are important microbial compo- of bacterial adhesion. nents of the ecosystem in the human oral cavity (Chapter 8, J. 0. Cisar). A discussion of the mycobacterial hemagglutinin and OTHMAR GABRIEL its appearance during various developmental stages of
Vols. 114 and I 15, Diffraction Macromolecules. Edited by H.
Methods in Enzymology, Methods for Biological
W.
WYCKOFF,
C.
H.
W.
HIRS,
AND
S. N.
TI-
Academic Press, New York, 1985. Vol. 114, $64.00; Vol. 115. $55.00. MASHEFF
This two-volume addition to Methods in Enzymology signals that protein crystallography has become an essential part of modern biochemistry. The editors’ goals have been to give biochemists an introduction to the field of macromolecular structure determination by X-ray diffraction, and to give crystallographers a comprehensive summary of techniques available to them. The first volume deals with the experimental aspects from crystal growth to X-ray data measurement. The second describes the analysis of these data. methods of phase determination, and refinement of the resulting structure, with a final section on the presentation and analysis of the structure. Because of the highly technical nature of this subject, browsing biochemists will not find too much here that is readily comprehensible, although there are a few chapters, such as Max Perutz’s fascinating description of the early days of protein crystallography, that are universally interesting. The suspicion with which protein crystallographers were regarded by their small molecule contemporaries would have made Perutz today an unlikely candidate for an NIH grant, and it is a tribute to the wisdom of the British Medical Research Council that
they nurtured this infant science until it could prove itself. Perutz also makes an important point that is just as relevant today when he disposes of the legend that the structures of hemoglobin and myoglobin were solved with primitive instruments in a hut near the Cavendish Laboratory. In fact they used the best and newest equipment that was available, including one of the world’s first electronic computers. For the crystallographer, however, this will become an essential handbook, not because it contains anything particularly new, but because, in the spirit of the Methods series, it contains everything in one place. Everything is here from crystallization to instructions on how to prepare drawings of a protein structure that can be understood by medical students. In fact, some exercise of editorial restraint might have shortened the text somewhat, although some of the museum articles make most enjoyable reading. Some other aspects of the editing are more annoying, in particular the rather large number of spelling errors. Examples such as Lease Squares and Duck University, together with the existence of several versions of some authors’ names in the index mar an otherwise most valuable text. Nevertheless, these two volumes will provide the essence of what every protein crystallographer needs, at least until the next major technical advance occurs, when it will become time for the next volume. DAVID R. DAVIES