The major credit for these volumes clearly rests with the authors of each entry. They are all recognized as being amongst those pre-eminent in their field. We wish to thank each of these authors for their excellent contribution and for their willingness to produce entries to tight deadlines. An additional 'thank you' is also due to the many contributors who provided suggestions and constructive criticism regarding the encyclopedia.

Our task as editors was helped immeasurably by the participation of our outstanding Editorial Advisory Board. Their ability to 'name names', their comments regarding additions or modifications to the list of entries and their expert reviewing of manuscripts established a solid foundation upon which the encyclopedia could be built. We would particularly like to welcome Ian McConnell, Fritz Melchers, Fred Rosen, Emil Unanue and Harald von Boehmer to the Editorial Advisory Board for the second edition of the Encyclopedia.

We greatly thank the following members of Academic Press for the publishing services of editorial development support and production of both print and electronic versions:

Carey Chapman, Lorraine Parry, Sara Gorman, Heather Burroughs, Manjula Kariyawasam, Ed Pentz, Emma Parkinson, Helen Knapp, Debi Kruse, Peter Lord, and also to picture researcher Emma Krikler and indexer Jan Ross.

Finally, thanks to Jane, Joe, Tom and Jess for the inevitable sacrifices that they had to make during the preparation of this second edition of the encyclopedia.

Plate 1 Lymph node. (A) Section of mouse lymph node showing recirculating IgD+ B cells around their portal of entry. The high endothelial venules (H) located in the T zone (T) are stained blue. IgD+ cells are also seen in the walls of the intranodal lymphatics on the edge of the T zone and in the follicles (F). En route to the follicles recirculating B cells travel along the walls of the intranodal lymphatics (arrows) where encounter with antigen from the lymph may occur. (B) Section of a formalin-fixed rat lymph node demonstrating large numbers of plasma cells in the medullary cords (M). These are stained brown with anti-Ig. Formalin-fixation has destroyed the surface Ig on the B cells. T - T zone; F - follicle; E - efferent lymphatic. (Kindly provided by Ian MacLennan, University of Birmingham Medical School, UK. Reproduced from MacLennan et al., 1997, Immunological Reviews 156, 53-66 with permission.)

Plate 2 Bone marrow. Trephine biopsy from a 45 year old man (Haematoxylin and eosin stain) Trephine biopsy examination of bone marrow is used commonly to diagnose both hematological and nonhematological conditions. (Kindly provided by Michael Watts, University college Hospitals, London, UK with permission.)

Clefted Lymphocytes

Plate 3 Lymphocyte, neutrophil and monocyte. Bottom left is a small lymphocyte, center is a polymorphonuclear neutrophil and top right is a monocyte showing the characteristic 'horseshoe-shaped' nucleus and moderately abundant pale cytoplasm. Two additional neutrophils are partly in the field of view at the top right. Romanowsky stain. (Kindly provided by the Michael Watts, University College Hospitals, London, UK with permission.)

Plate 4 Tonsil. Section of a normal human palatine tonsil. At upper right (pink) is the stratified squamous epithelium of the surface of the tonsil. This epithelium is highly folded. Beneath it is a collagen fiber layer (blue). At lower center is the lymphoid tissue (red). Apart from the pair of palatine tonsils, there is a pair of lingual tonsils and a pair of pharyngeal tonsils (adenoids) which contribute to the Waldeyer's ring of lymphoid tissue. (With permission from Photo Science Library.)

Antibody Stereoview

Plate 5 Antibody binding to a hapten. Stereo view of the 40-50 antibody combining site with VL on the left and VH on the right and colored to display concave (dark gray) and convex (green) molecular surfaces. The 40-50 binding site is a groove mostly on the surface of the light chain. The bound hapten, ouabain, is shown in yellow. (Kindly provided by Steven Sheriff, Bristol-Myers Squibb Pharmaceuticals Research Institute, Princeton, USA. Reproduced from Jeffrey et al, 1995, Journal of Molecular Biology 248, 344-360 with permission.)

Plate 6 Antibody paratope. (A) Stereo diagram of a ribbon structure of the VH: VL domain showing the side-chains of the contact residues that comprise the paratope of the N10 anti-Staphylococcal nuclease antibody. The heavy chain is colored green, the light chain yellow, CDR regions silver and contact residues (with side-chains shown) are magenta. Figure produced with RIBBONS (Carson 1991). (B) Contact molecular surface (cyan dots) of the N10 antibody (blue with contact residues in yellow) calculated by the method of Connolly (1983) and displayed using GRASP (Nicholls et al 1991.) Note the U-shape of the contact surface with the single heavy chain CDR3 contact residue Asn H-96 located just inside the open end of the U. (C) The N10 antibody paratope with the light chain on the left. Surface representation of the calculated AG residue contribution to binding by the N10 antibody and ihe Staphylococcal nuclease antigen residues. A color scale was constructed of the AG residue values, from blue (—2.0 kcal/mol) to red ( + 2.0kcal/mol). Thus, blue colors represent negative ("attractive") residue contributions, red colors represent positive ("repulsive") contributions. Figure produced with GRASP (Nicholls et al 1991). (Kindly provided by Steven Sheriff, Bristol-Myers Squibb Pharmaceuticals Research institute, Princeton, USA. Reproduced from Bossart-Whitaker et al., 1995, Journal of Molecular Biology 253, 559-575 with permission.)

Plate 7 (A) Addison's Disease. Adrenal gland from patient with Addisons disease, showing atrophy of the cortex and infiltration with mononuclear cells. (B) Another area from same adrenal gland, photographed at higher magnification. (Kindly provided by P E Bigazzi, University of Conneticut Health Center, USA with permission.)

Molecular Allergens

Plate 8 Allergens. Molecular modeling of the cockroach calycin allergen, Bla g 4. The Ca backbone structures for two models of Bla g 4 (designated bg12A-1 and bg12A-2) were modeled on the X-ray crystal coordinates for butterfly bilin-binding protein (BBP) and are compared with rat urinary protein allergen (RUP), for which the X-ray crystal structure has also been determined. The yellow spheres are conserved amino acid residues that form motifs which define the ligand-binding proteins, or calycins. (Kindly provided by M D Chapman, University of Virginia, USA with permission.)

Plate 9 Antibody-antigen interaction. (A) Conformational differences in antibody D1.3 VL CDR3 induced by differing antigen side-chains. Hen egg lysozyme (HEL) residue Gln121 makes two main-chain hydrogen bonds; to the carbonyl oxygen of D1.3 VL Phe91 and the amide nitrogen of D1.3 VL Ser93. Replacement of the glutamine by histidine in Turkey egg lysozyme (TEL) induces a conformational change in the backbone of VL CDR3 which allows the formation of a hydrogen bond between the histidine and the carbonyl oxygen of VL Trp92. (B) The effect of a Trp-Asp mutation on the interaction surface area of the D1.3-HEL complex (dots) and the mutant D1.3-HEL surface (solid line) demonstrates the loss of interaction surface area in the mutant complex. A 150 A2 loss in surface area accounts for the reduction in affinity of the mutant D1.3-HEL reaction. (C) Hydrogen bonding network of the D1.3-HEL interface mediated by bound solvent molecules; 25 water molecules form hydrogen bonds linking the antibody and antigen, directly or through other water molecules. (D) Water molecules in contact with the D1.3-HEL buried surface. Including the 25 bridging water molecules, nearly 50 solvent sites are in contact with the buried surface defined by the D1.3-HEL interface. Many of these water molecules fill internal cavities, further stabilizing the complex. (Kindly provided by B C Braden and R J Poljak, Center for Advanced Research in Technology, USA with permission.)

Plate 10 HLA-A2. The residues forming the domain interfaces are highlighted in color on the Ca backbone stereogram. Filled and colored Ca atoms make contacts <4 A. Red, a1; a2 residues in interface with b2M; green, b2M residues in interface with a^2; blue a3 residues in interface with b2M; yellow, b2M residues in interface a3; pink, a1a2 residues in interface with a3; orange, a3 residues in interface with a1a2. (A) A view perpendicular to a1a2 pseudodyad with the binding cleft viewed end-on (a1a2-a3 interface not shown). (B) A side view with the molecule rotated 90° about the pseudodyad (a3-b2M interface not shown). (Reprinted with permission from Saper MA, Bjorkman PJ and Wiley DC (1991) Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution. Journal of Molecular Biology 219: 277-319.)

Plate 11 CD8. Three-dimensional molecular model of the N-terminal region of a CD8 homodimer consisting of two a chains; (A) ribbon presentation, (B) stick presentation. The structural data for the N-terminal 113 amino acids are based on crystallography (protein data base: 1CD8). The three-dimensional model for each monomer was generated with RasMol version 2.5 (Roger Sayle, Greenford, Middlesex, UK), and the two monomers were combined as described (Leahy et al. (1992) Cell 68: 1145). The color coding represents groups; blue corresponds to the CDRl-like loop, light blue to the CDR2-like loop, and lime to the CDR3-like loop. The monomers are distinguished in brightness of color. (Kindly provided by GF Weber and H Cantor, Dana-Faber Cancer Institute, USA with permission.)

Plate 13 Monoclonal antibodies to lysozymes. Hen egg white lysozyme in complex with the Fab fragments of monoclonal antibodies raised against it. An exploded-view collage indicating how three different anti-lysozyme Fab's interact with lysozyme (center) in the x-ray structures of their respective complexes. The proteins are represented by their Ca chains and their interacting surfaces are outlined by juxtaposed dot surfaces. Note that the three crystal structures on which this diagram is based each contain only one Fab species; the Fabs do not crystallize together. (Photograph courtesy of Steven Sheriff and David Davies, NIH, USA.)

Plate 14 High endothelial venules in lymph node. (A) Rat mesenteric lymph node. Composite of about 200 scanning electron micrograph images. The capsule and the marginal sinus (MS) are seen at the top. The high endothelial venules (HEVs) are distributed mainly in the inner cortex and further in the interfollicular areas. The lymphatic labyrinths filled with lymphocytes are demonstrated in the inner cortex. S. medullary sinus. The lymphatic labyrinths and medullary sinuses are tinged in pale and dark blue, respectively. (B) Fractured portion of the inner cortex. An HEV is longitudinally opened at the lower left. The lymphatic labyrinth (L.L.) is shown near the HEV. (Kindly provided by Yechen He, Harbin Medical University, China, with permission.)

Plate 15 Germinal center. (a, b) Follicular T cell numbers rapidly increase during germinal center development. In a non-responding spleen (a) T cells in the white pulp are largely confined to the T zone (T) with only occasional T cells in the follicles (F); red pulp (R). (b) 7 days after primary immunization with antigen large numbers of T cells are found within the developing germinal center and surrounding follicular mantle - up to 10% of these have incorporated the thymidine analogue BrdU during a 2-hour pulse indicating that they are in cell cycle. (c, d) A pulse chase experiment where centrobtasts in the dark zone (D) of a rat splenic germinal center are labeled during a 5-hour pulse with BrdU. In panel c the spleen is taken at the end of the pulse when almost all centroblasts are labeled but the majority of centrocytes in the light zone (L) are not labeled. The spleen in d was taken 7 hours later when centrocytes derived from the proliferating centroblasts are labeled. F - follicular mantle; M - marginal zone; T - T zone. (Kindly provided by Ian MacLennan, University of Birmingham Medical School, UK. Reproduced from MacLennan et al, 1997, Immunological Reviews 156, 53-66 with permission.)

Plate 16 Delayed-type hypersensitivity. Brucellosis. Delayed-type hypersensitivity (DTH) reaction in the finger following needlestick injury. When vaccinating cattle, veterinarians are prone to needle stick injury. In those who have been sensitized by previous infection, albeit subclinical, this can be followed within 24-48h by a DTH reaction which ranges from the local reaction shown here, to a severe, generalized response which resembles many aspects of the infection itself. (Photograph courtesy K Hughes and the late J Forbes.)

Wild-Type LTtx-Deficient

Plate 17 Lymphotoxin knockout mice. Absence of germinal centers in mice lacking lymphotoxin a (LTor'~ mice). Wild-type (left panel) and (right panel)

mice were immunized intra-peritoneally with 108 sheep red blood cells and 10 days later spleen sections were analyzed by staining with the germinal center marker peanut agglutinin (blue) and with anti-IgD (brown). (Kindly provided by David Chaplin, Washington University School of Medicine, USA. Reproduced from Matsumoto, M et al. 1997, Immunological Reviews 156, 137-144 with permission.)

Plate 18 Cutaneous anaphylaxis. (A) (above left) Acute urticaria with marked erythema and whealing. (B) (above) Urticaria showing central clearing and an annular pattern. (C) (left) Symptomatic dermographism, marked linear whealing has occurred at sites of scratching. (Kindly provided by MHA Rustin and CH Ortey, The Royal Free Hospital, UK.)

Plate 19 H-2K polymorphism. Ribbon diagrams of the H2-Kb molecule with the vesicular stomatitis virus 8mer (RGYVYQGL) bound. Polymorphic residues in the a1 domain (exon 2) are highlighted in blue, a2 (exon 3) in red, and a3 (exon 4) in purple. (A) T cell receptor view of the complex. (B) (right) side view of the molecule. (Kindly provided by JA Frelinger and EJ Collins, University of North Carolina, USA with permission.)

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