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Chapter 48 : Hepatitis A Virus

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Hepatitis A Virus, Page 1 of 2

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Abstract:

Hepatitis A is an acute, self-limiting infection of the liver by hepatitis A virus (HAV), an enterically transmitted, hepatotropic member of the picornavirus family. Although HAV infection may occasionally result in fulminant hepatitis and death, it is not recognized to cause persistent infection or chronic hepatitis, even in severely immunocompromised individuals.

Citation: Williford S, Lemon S. 2017. Hepatitis A Virus, p 1165-1188. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Fourth Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819439.ch48
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Image of FIGURE 1
FIGURE 1

Electron micrographs of HAV. (A) Immune electron micrograph of HAV particles from human stool reacted with convalescent serum. The particles are heavily coated with and aggregated by antibody. Both “full” and “empty” particles can be seen. (B) An immune electron micrograph showing particles from human stool reacted with a preinfection serum. The 27- to 28-nm particles are nearly devoid of antibody and some fine structure can be seen. (C) Quasi-enveloped eHAV particles (panels a–d) and a nonenveloped HAV virion purified by density gradient centrifugation from supernatant fluids of infected Huh-7 cell cultures. The density of the fractions containing the particles is shown below the images. (A) and (B) Reprinted from Richman DD, Whitley RJ, Hayden FG (ed) , 3rd ed, with permission. (C) (Reprinted from reference with permission of the publisher.)

Citation: Williford S, Lemon S. 2017. Hepatitis A Virus, p 1165-1188. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Fourth Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819439.ch48
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Image of FIGURE 2
FIGURE 2

HAV genome organization and polyprotein processing cascade. The positive-strand RNA genome of HAV is approximately 7.5 kilobases (kb) in length and contains a single long open reading frame (ORF, box) flanked by relatively short 5′ and 3′ untranslated regions (UTRs, solid lines) as shown. The 5′ UTR is covalently linked at the 5′ end to the genome-linked protein VPg (otherwise known as 3B), and contains a highly structured internal ribosome entry site (IRES) that drives 5′ cap-independent translation of the polyprotein encoded by the ORF. The 3′ UTR terminates in a lengthy poly(A) sequence. The HAV polyprotein is co- and posttranslationally processed by the viral protease 3C (red box) that cleaves the polyprotein and its derivatives at sites indicated by the red triangles, producing both the structural (P1, turquoise) and nonstructural proteins (P2+P3, tan and red) that go to form the capsid and replicase complex, respectively. Yet-to-be-identified protease activities cause a final maturation cleavage in the VP0 (VP4+VP2) capsid protein, and trim the C-terminal pX domain off of VP1, during late stages in viral maturation.

Citation: Williford S, Lemon S. 2017. Hepatitis A Virus, p 1165-1188. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Fourth Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819439.ch48
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Image of FIGURE 3
FIGURE 3

X-ray crystallographic structure of the HAV capsid. Overall structure of the HAV capsid as deduced from X-ray crystallographic studies of formalin-inactivated vaccine virus (27). (A) Left: Accessible surface of the capsid, showing residues contributed by VP1 as red, VP2 green, and VP3 blue (60 copies of each are present within one capsid). VP4 is internal and is not seen. Right: Electrostatic surface of the capsid; red=negative charge, blue=positive charge, white=neutral. Yellow dots are sulfate ions. (B) Overlay of folded VP2 structure of HAV with that of VP2 protein from (left) cricket paralysis virus (CrPV) and (right) the mammalian picornavirus, foot-and-mouth virus (FMDV), showing prominent domain-swap paralleling structure in the insect virus. (C) Structural phylogeny of the HAV capsid showing its intermediate position between that of other mammalian picornaviruses and distantly related viruses such as CrPV. (Reprinted from reference with permission of the publisher.)

Citation: Williford S, Lemon S. 2017. Hepatitis A Virus, p 1165-1188. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Fourth Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819439.ch48
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Image of FIGURE 4
FIGURE 4

Biogenesis of quasi-enveloped eHAV virions (11). Several hypothetical mechanisms may account for the release of quasi-enveloped virions from hepatocytes. The most likely mechanism for eHAV biogenesis involves (a) the recruitment of assembled intracellular HAV capsids to cytoplasmic multivesicular bodies (MVBs) by protein components of the cellular ESCRT (ndosomal orting omplex equired for ransport) system such as ALIX, followed by the budding of capsids into MVBs such that they become enclosed in membranes within the MVB. Movement of the MVB to the plasma membrane and fusion of the outer MVB membrane and plasma membrane then delivers eHAV to the extracellular environment. Alternatively, (b) ESCRT-associated proteins might mediate release of eHAV directly at the plasma membrane. A third possibility (c) is that HAV capsids are engulfed in autophagosomes for transport to either MVBs or the plasma membrane. Loss of the eHAV membrane after egress from the cell (d) leads to the production of naked, nonenveloped virions. (Reprinted from reference with permission of the publisher.)

Citation: Williford S, Lemon S. 2017. Hepatitis A Virus, p 1165-1188. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Fourth Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819439.ch48
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Image of FIGURE 5
FIGURE 5

HAV replication cycle. (a) HAV interacts with a cellular receptor (possibly HAVCR1/TIM-1) at the basolateral membrane of the hepatocyte, is internalized, and (b) the viral genome is released into the cytoplasm; (b) the positive-strand RNA genome is translated in a cap-independent IRES-driven manner, resulting in a polyprotein that is (d) proteolytically processed to generate nonstructural proteins involved in genome replication (2B, 2C, 3AB, 3D) and the protease (3C), as well as capsid proteins (see Fig. 2 ). Changes in intracellular membranes are induced by 2BC, resulting in assembly of the nonstructural proteins into a membrane-bound replicase complex that (e) directs the synthesis of a complementary minus-strand RNA intermediate (blue) that is then used as template to (f) generate multiple new copies of positive-strand RNA (red). These newly synthesized positive-strand RNAs can (g) be directed to engage in additional translation or RNA synthesis or (h) packaged into capsids to generate intracellular viral progeny. These newly assembled viral particles (i) are recruited to multivesicular bodies for ultimate release from the infected cells across either (j) the apical plasma membrane into the biliary canaliculus (as shown) or across the basolateral membrane into the hepatic sinusoids (not shown). (Adapted from Martin A, Lemon SM, 2006 with permission of the publisher.)

Citation: Williford S, Lemon S. 2017. Hepatitis A Virus, p 1165-1188. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Fourth Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819439.ch48
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Image of FIGURE 6
FIGURE 6

Composite graph depicting HAV infection in an intravenously inoculated, experimentally infected chimpanzee (105). (A) Innate immune response: minimal increases in serum IFN-α occur during the first weeks of the infection in association with the transient presence of plasmacytoid dendritic cells (pDCs) in liver sinusoids and minimal intrahepatic expression of interferon-stimulated genes (ISGs) such as IFIT1 and ISG15. These early responses diminish prior to the peak in viral replication. (B) Intracellular cytokine staining shows that the virus-specific CD4+ T cell response (bottom) is more robust than the virus-specific CD8+ T cell cytokine or tetramer-specific response (top), and that the CD4+ T cell response correlates better with viral control. (C) IgM and total anti-HAV antibody responses detected in enzyme-linked immunosorbent assays. The total anti-HAV is measured in a blocking assay, where 100% indicates high-titer antibody. (D) Relative viral RNA abundance (GE=genome equivalents) in serum, liver tissue, and feces determined by reverse transcription polymerase chain reaction assays. Results are layered onto serum alanine transferase values that show a sharp spike indicative of acute liver injury at 4 weeks post inoculation. (Reprinted from reference with permission of the publisher.)

Citation: Williford S, Lemon S. 2017. Hepatitis A Virus, p 1165-1188. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Fourth Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819439.ch48
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Image of FIGURE 7
FIGURE 7

Electron micrographs of a marmoset hepatocyte during acute hepatitis A. The arrows in the upper panel point to cytoplasmic vesicles containing probable HAV capsids. The lower panel is a higher powered view of one of the vesicles more clearly showing viruslike particles. Bar=500 nm in the upper panel and 100 nm in the lower. Courtesy of Yohko Shimizu.

Citation: Williford S, Lemon S. 2017. Hepatitis A Virus, p 1165-1188. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Fourth Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819439.ch48
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Image of FIGURE 8
FIGURE 8

Photomicrograph of a liver section from a patient with acute hepatitis A, showing inflammation of the portal and periportal areas by lymphocytes coupled with lobular disarray and hepatocellular ballooning degeneration (cytoplasmic vacuolization). (Hematoxylin and eosin stain; original magnification 40x). (Adapted from Martin A, Lemon SM, 2006 with permission of the publisher.)

Citation: Williford S, Lemon S. 2017. Hepatitis A Virus, p 1165-1188. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Fourth Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819439.ch48
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Image of FIGURE 9
FIGURE 9

Estimated global prevalence of hepatitis A virus, 2005. (Reprinted from reference with permission of the publisher.)

Citation: Williford S, Lemon S. 2017. Hepatitis A Virus, p 1165-1188. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Fourth Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819439.ch48
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Image of FIGURE 10
FIGURE 10

Estimates of anti-HAV seroprevalence by age group and selected populations in different world regions, 1990 and 2005. Groups shown include those in Western Europe, South sub-Saharan Africa, North America (high income), and Oceania. The impact of changing standards of sanitation and immunization programs is evident in shifts in age-specific prevalence of anti-HAV antibody. No changes were estimated to have occurred in the African region. (Adapted from reference with permission of the publisher.)

Citation: Williford S, Lemon S. 2017. Hepatitis A Virus, p 1165-1188. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Fourth Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819439.ch48
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Image of FIGURE 11
FIGURE 11

Natural history of hepatitis A. The infection is typically acute in nature, with symptoms and signs of the infection usually occurring within 3 to 5 weeks of exposure. The sequence of events includes shedding of infectious HAV in feces and viremia, followed by increases in serum ALT activity (red line), and the appearance of IgM and IgG anti-HAV antibody responses (the latter typically measured as total anti-HAV antibody). (Adapted from Martin A, Lemon SM, 2006 with permission of the publisher.)

Citation: Williford S, Lemon S. 2017. Hepatitis A Virus, p 1165-1188. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Fourth Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819439.ch48
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References

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