1887

22 Cell Biology of Virus Infection

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.

Ebook: Choose a downloadable PDF or ePub file. Chapter is a downloadable PDF file. File must be downloaded within 48 hours of purchase

Buy this Chapter
Digital (?) $30.00

Preview this chapter:
Zoom in
Zoomout

22 Cell Biology of Virus Infection, Page 1 of 2

| /docserver/preview/fulltext/10.1128/9781555817633/9781555813024_Chap22-1.gif /docserver/preview/fulltext/10.1128/9781555817633/9781555813024_Chap22-2.gif

Abstract:

This chapter focuses on events in viral replication cycles that have similarity or relevance to the interactions of bacterial pathogens with cells, and the examples discussed will draw mainly on membrane-containing enveloped viruses. The transferrin receptor is a well-studied cellular protein that undergoes constitutive endocytosis through clathrin-coated vesicles (CCVs). Phagocytosis plays a key role in the clearance of cells infected by viruses, either following antibody or cell-mediated killing of these cells or after apoptosis of the cell in response to the virus infection. Macropinocytosis is similar to phagocytosis in that it is dependent on remodeling of cortical actin, but it is not dependent on the ligation of specific receptors. Viral fusion proteins can be grouped into several distinct classes based on the organization of the protein. Class 1 fusion proteins, which include influenza HA and HIV envelope glycoprotein (Env), are synthesized as single-chain transmembrane proteins that assemble into trimers in the ER of the infected cell. Within these factories, viral DNA and protein synthesis occur and progeny viral particles undergo assembly. Virus replication is tightly integrated into the properties of the host cell. Due to their ability to efficiently exploit specific cellular functions, viruses have been, and continue to be, very effective tools to study basic cellular functions. Indeed, virus systems of one sort or another underlie much of the current knowledge of molecular genetics and cell biology.

Citation: Marsh M. 2004. 22 Cell Biology of Virus Infection, p 517-542. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch22

Key Concept Ranking

Equine infectious anemia virus
0.49157503
Mouse mammary tumor virus
0.4904778
Human immunodeficiency virus 1
0.47966915
0.49157503
Highlighted Text: Show | Hide
Loading full text...

Full text loading...

Figures

Image of Figure 22.1
Figure 22.1

Cartoon of herpesvirus assembly. Herpesviruses use both protein coats and lipid membranes to generate free virus particles. Capsids assemble in the nucleus of the infected cell and bud through the inner nuclear membrane to generate a transient enveloped particle in the space between the inner and outer nuclear membranes (this space is continuous with the lumen of the ER). These enveloped particles are then believed to fuse with the outer nuclear/ER membrane to deliver the capsid to the cytoplasm. Subsequently the capsids acquire virally encoded tegument proteins that are available in the cytoplasm and undergo a second envelopment step into a cytoplasmic membrane-bound compartment. The tegument proteins form a layer between the protein shell of the capsid and the membrane. Subsequently, viruses are released from the cell when the virus-containing vesicles fuse with the plasma membrane.

Citation: Marsh M. 2004. 22 Cell Biology of Virus Infection, p 517-542. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch22
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 22.2
Figure 22.2

Virus entry. Entry mechanisms for animal viruses. Direct fusion or penetration at the plasma membrane, seen for many pH-independent viruses, e.g., HIV. Endocytosis of viruses in clathrin-coated vesicles and fusion or penetration from endosomes as seen for many pH-dependent viruses, e.g., SFV. Endocytosis in non-clathrin-coated vesicles that also leads to delivery to endosomes and provides an alternative route for some pH-dependent viruses, e.g., influenza virus. Uptake through caveolae and delivery to caveosomes as observed for SV40.

Citation: Marsh M. 2004. 22 Cell Biology of Virus Infection, p 517-542. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch22
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 22.3
Figure 22.3

Fusion proteins. Cartoon showing the domain organization of viral fusion proteins. The shaded boxes indicate fusion peptides. HIV, human immunodeficiency virus; SU, surface unit; TM, transmembrane; SFV, Semliki Forest virus (); TBE, tick-borne encephalitis virus ().

Citation: Marsh M. 2004. 22 Cell Biology of Virus Infection, p 517-542. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch22
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 22.4
Figure 22.4

pH-induced conformational changes in influenza HA. (1) Mature influenza HA is a trimer of 3 × HA1 × 3 × HA2 subunits (derived from the precursor 3 × HA by proteolytic cleavage). The HA1 subunits contain the sialic acid-binding pockets involved in receptor recognition. (2–4) Following exposure to low pH, the HA1 subunits dissociate (but remain linked to their respective HA2 subunit via and an S–S bond), releasing the clamp that maintains the metastable neutral pH form of HA2. (3) The extended loop in HA2 adopts a helical formation and in so doing moves the N-terminal helical domain (shaded) and fusion peptide (dark gold) to the top of the long α-helix (light gold). (4) Subsequently, the dark gold helix is believed to fold back on the light gold helix to form the six-helix bundle that brings the N and C termini of the protein, which are embedded in the host cell and viral membranes, respectively, close together to drive merger of the two membrane systems.

Citation: Marsh M. 2004. 22 Cell Biology of Virus Infection, p 517-542. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch22
Permissions and Reprints Request Permissions
Download as Powerpoint

References

/content/book/10.1128/9781555817633.chap22
1. Greber, U. F. 2002. Signalling in viral entry. Cell. Mol. Life Sci. 59:608626. Recent review on signaling pathways activated by viruses during entry into cells.
2. Greber, U. F.,, and A. Fassati. 2003. Nuclear import of viral DNA genomes. Traffic 4:136143. Recent review on targeting of incoming viral genomes to the nucleus.
3. Heath, C. M.,, M. Windsor,, and T. Wileman. 2001. Aggresomes resemble sites specialized for virus assembly. J. Cell Biol. 153:449455. Study of the organization of cytoplasmic replication sites for a large DNA virus.
4. Johnson, D. C.,, and M. T. Huber. 2002. Directed egress of animal viruses promotes cell-to-cell spread. J. Virol. 76:18. Discussion of the mechanisms of cell-to-cell transfer of viruses.
5. Knipe, D. M.,, P. M. Howley,, D. E. Griffin,, R. A. Lamb,, M. A. Martin,, B. Roizman,, and S. E. Straus (ed.). 2001. Fields’ Virology, 4th ed. Lippincott Williams & Wilkins, Philadelphia, Pa. Standard virology text.
6. Kooyk, Y.,, B. Appelmelk,, and T. B. Geijtenbeek. 2003. A fatal attraction: Mycobacterium tuberculosis and HIV-1 target DC-SIGN to escape immune surveillance. Trends Mol. Med. 9:153159. Review of the role of a C-type lectin, DC-SIGN, in viral and bacterial pathogenesis.
7. Marsh, M.,, and H. McMahon. 1999. The structural era of endocytosis. Science 285:215220. Review of interactions between proteins implicated in clathrin-mediated endocytosis.
8. McDonald, D.,, M. A. Vodicka,, G. Lucero,, T. M. Svitkina,, G. G. Borisy,, M. Emerman,, and T. J. Hope. 2002. Visualization of the intracellular behavior of HIV in living cells. J. Cell Biol. 159:441452. Study of cellular mechanisms used by incoming HIV particles to aid transport to the nucleus. Implicates both actin and tubulin-based cytoskeletal systems.
9. Meier, O.,, K. Boucke,, S. V. Hammer,, S. Keller,, R. P. Stidwill,, S. Hemmi,, and U. F. Greber. 2002. Adenovirus triggers macropinocytosis and endosomal leakage together with its clathrin-mediated uptake. J. Cell Biol. 158:111911131. Study of adenovirus entry via endocytosis. Indicates that infectious particles are internalized by clathrin-mediated endocytosis, but induce macropinocytosis. Moreover, this macropinocytic activity is required for penetration and viral replication.
10. Pelchen-Matthews, A.,, B. Kramer,, and M. Marsh. 2003. Infectious HIV-1 assembles in late endosomes in primary macrophages. J. Cell Biol. 162:443455. Demonstration that infectious HIV particles are assembled in late endosomes in infected macrophages.
11. Pornillos, O.,, J. E. Garrus,, and W. I. Sundquist. 2002. Mechanisms of enveloped RNA virus budding. Trends Cell Biol. 12:569579. Review of recent work on the assembly of enveloped viruses and the role of cellular ESCRT proteins in these events.
12. Rietdorf, J.,, A. Ploubidou,, I. Reckmann,, A. Holmstrom,, F. Frischknecht,, M. Zettl,, T. Zimmermann,, and M. Way. 2001. Kinesin-dependent movement on microtubules precedes actin-based motility of vaccinia virus. Nat. Cell Biol. 3:9921000. Study of the role of microtubule-mediated translocation in vaccinia virus release.
13. Sodeik, B. 2000. Mechanisms of viral transport in the cytoplasm. Trends Microbiol. 8:465472. Review of cellular transport systems used by viruses to facilitate entry, infection, and release.

Tables

Generic image for table
Table 22.1

Genetic composition and coat structures of different viruses

Citation: Marsh M. 2004. 22 Cell Biology of Virus Infection, p 517-542. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch22
Generic image for table
Table 22.2

Examples of cellular receptors used by viruses

Citation: Marsh M. 2004. 22 Cell Biology of Virus Infection, p 517-542. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch22
Generic image for table
Table 22.3

Examples of the pH dependence of entry of various virus families

Citation: Marsh M. 2004. 22 Cell Biology of Virus Infection, p 517-542. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch22

This is a required field
Please enter a valid email address
Please check the format of the address you have entered.
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error