Plate I Xvii: Figure 2A.2 Figure 2A.3

PLATE I
xvii
Figure 2A.2MCold sores at the pustular and crusting stages
Figure 2A.3MRose Bengal staining of herpes simplex virus dendritic ulceration in a grafted cornea. (Kindly provided by R. E. Bonshek and A. B. Tullo)
Figure 2C.4MProteins of CMV which have been mapped to date. UL = unique long region; US = unique short region; TR = terminal repeat; IR = inverted repeat. The genome is linear within the virus but has been circularized for convenience. Open reading frames of known function are coloured according to the following code: orange = transactivators; pink = DNA replication; green = capsid and/or assembly; red = tegument; pale blue = envelope; dark green = immune evasion; dark blue = miscellaneous
Principles and Practice of Clinical Virology, Fifth Edition. Edited by A. J. Zuckerman, J. E. Banatvala, J. R. Pattison, P. D. Griths and B. D. Schoub & 2004 John Wiley & Sons Ltd ISBN 0 470 84338 1
PLATE II
xviii
Figure 2C.8MSchematic representation of the ways viruses can interfere with presentation of HLA-peptide complexes at the plasma membrane. Rib, ribosome; ER, endoplasmic reticulum; V, virus-encoded protein; PRO, proteosome; PM, plasma membrane; TAP, transporter associated with antigen presentation. Peptides derived from virus-infected cells are generated in the proteosome and actively transported by TAP into the lumen of the ER. A ribosome is shown producing a protein with a signal peptide, which folds in the ER to produce the HLA Class I chain. This should normally associate with peptide and be transported to the plasma membrane. Misfolded HLA molecules can be re-exported from the lumen of the ER back into the cytosol where they are degraded by the proteosome. Virus-encoded genes interfere with this process as follows: the proteins may be inherently insusceptible to proteosome digestion (EBNA of EBV) or may be modied to reduce their digestion (pp65 acts on MIE protein of HCMV). Proteins may block the function of TAP (ICP47 of HSV; US6 of HCMV). Proteins may bind mature class I molecules within the ER and so sequester them (E3-19K protein of adenoviruses; US3 protein of HCMV; m152 protein of MCMV). Two proteins of HCMV (US2 and US11) facilitate the re-export from the ER to the cytosol of mature HLA class I molecules. If all of these mechanisms are completely successful, the level of HLA display at the PM will be insufcient to prevent NK cells or macrophages recognising the cell as being abnormal and so destroying it. Proteins/peptides encoded within HCMV (UL18) or MCMV (m144) are presented at the plasma membrane to act as a decoy for NK cells by providing a negative signal. In addition, HCMV UL16 blocks transmission of a positive signal to another group of NK cells
Figure 2D.7MPhotomicrograph of a MayGrunwaldGiemsa-stained peripheral blood lm from acute infectious mononucleosis. An atypical mononuclear cell is illustrated (x 1000)
PLATE III
xix
Figure 2F.5MGenome diagram of KSHV. Open boxes with Roman numbers denote groups of structural or metabolic genes which are conserved among herpesviruses and also many other herpesviruses. The solid line represents the long unique (coding) region, open and lled rectangles internal or terminal repeat regions. Solid circles represent originas of lytic relication [ori-(L), ori-(R)]. The position and transcriptional orientation of viral genes discussed in the text is indicated by pointed boxes. A red shading indicates genes known to be expressed in latently infected spindle cells and PEL cells (see text), light blue, dark blue and green shading refers to genes expressed in the different stages of the lytic cycle (see text). Colour coding of the names of individual viral genes refers to their presumed function, as indicated (see also text)
Figure 2F.6MExpression of vIL-6 in B cells of Multicentric Castlemans Disease. vIL-6 is expressed in a small number of KSHV-infected B cells, but may affect others through paracrine action (see text). Photograph kindly provided by Drs Y. Chang and P. Moore
PLATE IV
xx
Figure 2F.7MOverview of some KSHVencoded proteins that may contribute pathogenesis. Vital proteins are coloured in red, interacting cellular proteins in grey. See text for a detailed explanation of the pathways and receptors engaged by KSHV proteins
Figure 2F.8MKSHVencoded proteins involved in the control of apoptosis. Two apoptosis pathways exist in human cells and are regulated by a number of cellular and viral components. The extrinsic pathway is initiated by Fas-L or tumour necrosis factor (TNF) and assembly of the procaspase 8 complex is inhibited by FLIP (FLICEinhibitory protein; see text). A KSHVencloded FLIP homologue, vFLIP, acts in a similar manner. The intrinsic pathway is triggered by DNA damage, cytokine withdrawal, cytotoxic drugs and regulated by the Bcl/Bad/Bax group of proteins. A viral bcl-2 homologue, vbcl-2, acts at this stage. Finally, vIAP acts in the intrinsic pathway and on procaspase 3, as discussed in the text
PLATE V
xxi
Figure 8.1MSchematic graphic of adenovirus particle
PLATE VI xxii
Figure 11.3MA schematic representation of CD46 (MCP, membrane cofactor protein) (left), the major protein receptor for attenuated MV strains. MV binding sites are located within the short consensus repeat (SCR) domains 1 and 2, whereas complement components C3b/C4b bind to SCR 3 and 4, respectively. Proximal to the transmembrane domain, oligo-saccharide-rich serin/threonine/proline (STP) domains are located. CD150, a member of the lg superfamily, (right) is the receptor of all MV strains tested as yet. MV binding occurs at the membrane distal domain (the V domain). Glycosylation sites in the extracellular domains are indicated as are residues in the cytoplasmic domain identied as important for signaling
PLATE VII
xxiii
Figure 12.2MSchematic representation of the replication and translation of rubella virus structural and non-structural proteins. (Reproduced from Best, Cooray & Banatvala, Topley and Wilson, 10th edition)
PLATE VIII
xxiv
Figure 21.3MWorld distribution of rabies. Rabies free areas are white; red indicates terrestrial rabies with or without bat rabies, and countries with only bat lyssaviruses are green
Figure 24.4MGiant pronormoblast
PLATE IX
xxv
Figure 24.5MChildren with characteristic slapped cheek appearance and reticular lacy rash of fth disease
Figure 25A.8MPerivascular lymphocytic inltration in the central nervous system. (Courtesy of Dr Margaret Esiri)
PLATE X
xxvi
Figure 25A.9MUsing unstimulated, uncultured peripheral blood lymphocytes from a patient with HTLV-I associated myelopathy the accumulation of viral proteins at the cell-cell junction and subsequent transfer of gag proteins and HTLV-I nucleic acids to a CD4 lymphocyte from an uninfected donor is demonstrated (courtesy of Professor Charles Bangham)
PLATE XI
xxvii
Figure 28.3MRecent Emergence and Reemergence of Human Viral Diseases, Examples
Figure 28.4MWorld Distribution of Dengue 2002
PLATE XII
xxviii
Figure 28.5MNew World Hantaviruses

Plate I Xvii: Figure 2A.2 Figure 2A.3

Uploaded by

Copyright:

Available Formats

Plate I Xvii: Figure 2A.2 Figure 2A.3

Uploaded by

Document Information

Original Title

Copyright

Available Formats

Share this document

Share or Embed Document

Sharing Options

Did you find this document useful?

Is this content inappropriate?

Copyright:

Available Formats

Plate I Xvii: Figure 2A.2 Figure 2A.3

Uploaded by

Copyright:

Available Formats

PLATE I

Figure 2A.2MCold sores at the pustular and crusting stages

Figure 8.1MSchematic graphic of adenovirus particle

Figure 24.4MGiant pronormoblast

Figure 28.3MRecent Emergence and Reemergence of Human Viral Diseases, Examples

Figure 28.4MWorld Distribution of Dengue 2002

Figure 28.5MNew World Hantaviruses

You might also like