ICTVdB Virus Description - 00.001. Adenoviridae

Cite this publication as: ICTVdB Management (2006). 00.001. Adenoviridae. In: ICTVdB - The Universal Virus Database, version 3. Büchen-Osmond, C. (Ed), Columbia University, New York, USA

ICTVdB Virus Code: 00.001. Virus accession number: 00001FAM. Obsolete virus code: 01.; superceded accession number: 01000000.
NCBI Taxon Identifier NCBI Taxonomy ID: 10508.

Name, Synonyms and Lineage

Morphology

Electron micrograph of a Human adenovirus, courtesy of C. Büchen-Osmond . Additional images can bee found in the Picture Gallery.

Physicochemical and Physical Properties

Nucleic Acid

Proteins

Structural Proteins: Capsid protein S (II) forms the hexon monomer. Capsid protein has a molecular mass of 63 Mr x 10³ 109000 Da with 720 copies per virion (3 identical polypeptides per hexon, 240 hexons per capsid, is expressed in the late transcription phase (class L3, is located on the basal surface of the hexon forming the nucleocapsid. Capsid protein S (III, has a molecular mass of 63 kDa with five polypeptides interacting with each other to form the penton base 64 copies per virion; is expressed in the very late transcription phase (transcription class L2, is the surface protein (forming the penton base that is tightly associated with one or two fibers (IV), has been cleaved during post-translational processing from the precursor protein. Capsid protein IIIa is associated with the penton base (class L1, has a molecular mass of 64000 Da with 60 copies per virion (because five monomers are associated with each penton base, is expressed in the late transcription phase; is the surface protein (that is involved in penetration, has been cleaved during post-translational processing from the precursor protein; modifications during post-translational processes include phosphorylation. Capsid protein S (IV) forms the fibers (class L5) has a molecular mass of 62000 Da with 12 copies per virion (each made up of three polypeptides, is expressed in the very late transcription phase; is involved in the receptor binding process to susceptible host cell surface and exhibiting hemagglutination activity; which possess(es) toxin-like activity; modifications during post-translational processes include glycosylation. Inner capsid protein is a major core protein (possibly stabilizing the particle or involved in the assembly of virion, modifications during post-translational processes include phosphorylation. Inner capsid protein VIII, a minor hexon polypeptide has a molecular mass of 25000 Da; is expressed in the very late transcription phase (class L4, is forming the core (possible involved in stabilization or assembly of the particle, modifications during post-translational processes include phosphorylation. Fiber protein IV. Fiber protein modifications during post-translational processes include glycosylation. Core protein S (V), associated with DNA and penton base, is a minor core protein has a molecular mass of 42000 Da with 180 copies per virion. Core protein is expressed in the late transcription phase (class L2). Core protein is a basic protein that is non-covalently associated with the genome forming a "chromatin-like" substance. Core protein S (pVII), a major core protein; has a molecular mass of 22000 Da. Core protein is expressed in the late transcription phase (class L2). Core protein is histone-like and possibly involved in packaging. Core protein pX, X and µ has a molecular mass of 10000 Da (each). Core protein is expressed in the late transcription phase (class L2). Core protein Term or TP for terminal protein has a molecular mass of Mr 75 x 10³ 80000 Da (when obtained by SDS-PAGE). The core protein is expressed in the intermediate early transcription phase (class E2B). Core protein is binding DNA during genome replication; modifications during post-translational processes include phosphorylation.

Non-Structural Proteins: The virus codes for enzymes, or genome associated polypeptides; an DNA-dependent DNA polymerase. In addition to the polymerase, the virus codes for enzymes such as replicase and protease; 1 internal protein(s).

Lipids

Carbohydrates

Transcription of the Adenovirus genome is regulated by virus-encoded trans-acting regulatory factors. Products of the immediate early genes regulate expression of the early genes. Early genes are encoded at various locations on both strands of the DNA (l = "leftward strand" and r = "rightward strand"). Multiple protein products are made from each gene by alternative splicing of mRNA transcripts - splicing was first discovered in Adenoviruses.

Replication is divided into EARLY and LATE phases, the latter defined as beginning with the onset of DNA replication. Attachment to cells is rather slow, taking several hours to reach a maximum.

The process of intracellular uncoating of virions is understood. Virus uncoating occurs in the cytoplasm; the viral core is delivered to the cell nucleus; the site of mRNA transcription or DNA replication.

Infection and Replication: Host cell DNA synthesis is shut-off; early in the replication cycle. Host cell RNA and protein synthesis is shut-off; later in the replication cycle.

Transcription: Virus transcription is temporally regulated; 2 classes of genes recognized; they are termed EIA and E1B; E2A and E2B; E3 and E4 early and late (L1, L2 and L3; L4 and L5). The viral genome is transcribed from both DNA strands by host cell enzymes.

During the early stage, the viral genome is transcribed by eukaryotic nuclear RNA polymerase II; late stage, the viral genome is transcribed by eukaryotic nuclear RNA polymerase III. Cellular RNA polymerase III; encode products which facilitate translation; of late mRNAs. Viral genes are expressed from an early promoter (that is E1-E4, two intermediate), or a later promoter (L). Viral mRNA(s) is/are transcribed from four early E1-E4, two intermediate promoters and one major late (L) promoter 5 promoter(s, in an ambisense coding arrangement; all.

Primary transcripts are capped; polyadenylated. Viral mRNA families are produced by complex splicing patterns.

Coding Strategy of Segment 1: sequence encodes non-structural proteins. Sequence encodes protease.

Translation: Structural proteins, or non-structural proteins. Synthesized in the nucleus. Translation of structural proteins occurs during the early transcription phase of replication (TP), or intermediate transcription phase of replication (IX and IVa2), or late transcription phase of replication (II-VIII, X). Translation of non-structural proteins occur in the early stage of replication (DBP DNA pol and others), or late stage of replication (maturation 52/55kDA, mu, 33kDa p protein and 100 kDa). Structural proteins, or non-structural proteins (many). Are modified by post-translational processes. Including proteolytic cleavage, or phosphorylation, or glycosylation.

The genome replicates in the nucleus. Replication does not involve a reverse transcription step. Genome replication occurs by a strand-displacement. Genome replication uses a protein priming mechanism (terminal protein) (together with a), or virus-coded DNA polymerase (and), or DNA binding protein (in concert with), or cellular factors.

Virions may provide helper functions to dependent virus during replication. Virion acts as helper for a satellite virus.

Replication cycle The precursor of capsid protein is found in the infected cell nucleus. Viral proteins accumulate in the nucleus. Virions accumulate in the cell nucleus.

Assembly and Egress: Viruses assemble in the nucleus (sometimes in paracrystalline arrays along with similar arrays of virus structural proteins).

Maturation: Virions mature after proteolysis of some structural proteins by the virus-coded protease.

Release: Virus is released from host cell. Virus is released from host cell by disintegration.

Oligoprimer sequences for the virus are listed in the OligoVir database MP0410 .

Natural Host

Class Mammalia Order Scandentia, or Primates, or Perissodactyla, or Artiodactyla, or Rodentia;
Family Hominidae; virus infects Homo sapiens (human).

General Symptoms in Animals Infection can affect the respiratory system, or gastrointestinal system. General symptoms include conjunctivitis. Signs and symptoms include pharyngitis, or pneumonia; diarrhea (infants), or hepatitis or liver dysfunction (infants, liver transplant patients, carcinoma (in newborn hosts of heterologous species).

Severity and Occurrence of Disease

Transmission and Vector Relationships

Non-Vector Transmission:
Virus is transmitted through contaminated faeces; the likelihood of viral transmission by faecal-oral route (water and food-borne) is moderate; the likelihood of viral transmission by direct contact is moderate.

Experimental Hosts and Symptoms

Pathology

Cytopathology: Inclusions are present in infected cells (in later stage of infection as characteristic basophilic nuclear inclusions). Inclusion bodies are of diagnostic value. Inclusion bodies in the host cell are found in the nucleus. Other cellular changes include early rounding of cells and aggregation of chromatin. Images of Histopathological Changes

Electron micrograph of a thin section of infected cells Crystallized inclusions in infected cells. HeLa cells 24 hr after infection.

Geographical Distribution

Taxonomic Structure of the Family

Unassigned Viruses

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The description has been generated automatically from DELTA files.

ICTVdB - The Universal Virus Database, developed for the International Committee on Taxonomy of Viruses (ICTV) by Dr Cornelia Büchen-Osmond, is written in DELTA. The virus descriptions in ICTVdB are coded by ICTV members and experts, or by the ICTVdB Management using data provided by the experts, the literature or the latest ICTV Report. The character list is the underlying code. All virus descriptions are based on the character list and natural language translations from the encoded descriptions are automatically generated and formatted for display on the Web.

Developer of the DELTA software: M. J. Dallwitz, T. Paine and E. Zurcher

ICTVdB and DELTA related References

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