Physical organization of the enteric adenovirus type 41 early region 1A

The usefulness of the polymerase chain reaction (PCR) method for diagnosing adenovirus infections was investigated. Several primers, including primers specific for the hexon-coding region and for enteric adenovirus types 40 and 41, were evaluated. The PCR method was validated against cell culturing in routine diagnostic work and against restriction enzyme analysis of viral DNA. Sixty diagnostic specimens were selected for

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“…'The sequence position is from vanLoon et al(30). f The sequence position is from Allard and Wadell(2). 41AA142 _ 40AA45 _.…”

mentioning

confidence: 99%

Polymerase chain reaction for detection of adenoviruses in stool samples

et al. 1990

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“…Both of these constructs remained able to bind p300 in HeLa cell lysates ( Fig. 4, lanes 5 and 6); however, while 12S.DA21 showed an essentially wild-type level of p300-binding activity, 12S.LS20 consistently showed a much reduced level, suggesting that stable p300 association does involve specific residues in the small stretch from positions 15 to 25. Although there is little sequence conservation at the extreme N terminus of the ElA products, it is notable that all serotypically distinct ElA forms so far sequenced have an arginine at position 2, and several encode a histidine at position 3 (1,40,43,71,72) (Fig. 2).…”

Section: Resultsmentioning

confidence: 99%

“…However, the two active sites in this region are not limited to sequences within conserved regions 1 and 2; growth control activity requires the relatively nonconserved region at the extreme N terminus as well (41,66,69,79). The active site linked with conserved region 2 is supported by sequences in conserved region 1 (17,79) (Fig. 1).…”

mentioning

confidence: 99%

Identification of specific adenovirus E1A N-terminal residues critical to the binding of cellular proteins and to the control of cell growth

Wang

Rikitake

Carter

et al. 1993

J Virol

244

126

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Adenovirus early region 1A (E1A) oncogene-encoded sequences essential for transformation- and cell growth-regulating activities are localized at the N terminus and in regions of highly conserved amino acid sequence designated conserved regions 1 and 2. These regions interact to form the binding sites for two classes of cellular proteins: those, such as the retinoblastoma gene product, whose association with the E1A products is specifically dependent on region 2, and another class which so far is known to include only a large cellular DNA-binding protein, p300, whose association with the E1A products is specifically dependent on the N-terminal region. Association between the E1A products and either class of cellular proteins can be disrupted by mutations in conserved region 1. While region 2 has been studied intensively, very little is known so far concerning the nature of the essential residues in the N-terminal region, or about the manner in which conserved region 1 participates in the binding of two distinct sets of cellular proteins. A combination of site-directed point mutagenesis and monoclonal antibody competition experiments reported here suggests that p300 binding is dependent on specific, conserved residues in the N terminus, including positively charged residues at positions 2 and 3 of the E1A proteins, and that p300 and pRB bind to distinct, nonoverlapping subregions within conserved region 1. The availability of precise point mutations disrupting p300 binding supports previous data linking p300 with cell cycle control and enhancer function.

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“…While the long fiber binds to CAR, the receptor(s) of the short fiber, present in six trimeric copies per virion, is unknown. It has been speculated that the short fibers may be responsible for the exceptionally high selectivity of Ad41 for the digestive tract [35,36].…”

Section: The Coxsackie Virus B Adenovirus Receptor (Car)mentioning

confidence: 99%

Adenovirus endocytosis

Meier

Greber

2003

The Journal of Gene Medicine

177

123

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Pathogen entry into cells occurs by direct penetration of the plasma membrane, clathrin-mediated endocytosis, caveolar endocytosis, pinocytosis or macropinocytosis. For a particular agent, the infectious pathways are typically restricted, reflecting a tight relationship with the host. Here, we survey the uptake process of human adenovirus (Ad) type 2 and 5 and integrate it into the cell biology of endocytosis. Ad2 and Ad5 naturally infect respiratory epithelial cells. They bind to a primary receptor, the coxsackie virus B Ad receptor (CAR). The CAR-docked particles activate integrin coreceptors and this triggers a variety of cell responses, including endocytosis. Ad2/Ad5 endocytosis is clathrin-mediated and involves the large GTPase dynamin and the adaptor protein 2. A second endocytic process is induced simultaneously with viral uptake, macropinocytosis. Together, these pathways are associated with viral infection. Macropinocytosis requires integrins, F-actin, protein kinase C and small G-proteins of the Rho family, but not dynamin. Macropinocytosis per se is not required for viral uptake into epithelial cells, but it appears to be a productive entry pathway of Ad artificially targeted to the high-affinity Fcgamma receptor CD64 of hematopoietic cells lacking CAR. In epithelial and hematopoietic cells, the macropinosomal contents are released to the cytosol. This requires viral signalling from the surface and coincides with particle escape from endosomes and infection. It emerges that incoming Ad2 and Ad5 distinctly modulate the endocytic trafficking and disrupt selective cellular compartments. These features can be exploited for effective artificial targeting of Ad vectors to cell types of interest.

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Physical organization of the enteric adenovirus type 41 early region 1A

Cited by 18 publications

References 55 publications

Polymerase chain reaction for detection of adenoviruses in stool samples

Polymerase chain reaction for detection of adenoviruses in stool samples

Identification of specific adenovirus E1A N-terminal residues critical to the binding of cellular proteins and to the control of cell growth

Adenovirus endocytosis

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