Characterization of a canine adenovirus hemagglutinin

Abstract

MARUSYK, R. G., and T. YAMAMOTO. 1971. Characterization of a canine adenovirus hemagglutinin.Can. J. Microbial. 17: 151-155. The hemagglutinating activity of the canine adenoviruses was found to be more than 80y0 associated with both the intact and incomplete ('empty') virus particles, the remaining complete hemagglutinating activity being associated with a naturally occurring soluble penton dinier structure. Trypsin treatment of the heniagglutinin -red blood cell coniplex and receptor-competition experiments, using purified fiber component to block the receptor sites on the red blood cells, indicate that there are different receptors for infectious canine laryngotracheitis (ICL) virus and infectious canine hepatitis (ICH) virus.The ICL adenovirus was found to heniagglutinate human and rat erythrocytes but not those of a number of other animal species. Using human group '0' erythrocytes the ICL virus associated heniagglutinating activity was found to occur over a wide range in temperature and pH, and certain purification procedures, such as fluorocarbon treatment and sonic oscillation, were found to inactivate the hemagglutinin rapidly.

The Cell Adhesion Molecule “CAR” and Sialic Acid on Human Erythrocytes Influence Adenovirus In Vivo Biodistribution

“…Our data and numerous reports describing the ex vivo interaction of CAR-binding HAd5 with human/rat erythrocytes [12], [21]–[23], [29], [36], [51]–[53] strongly suggest this interaction probably occurs after the intravascular injection of CAR-tropic vectors. Notably, Lyons et al showed that that >90% HAd5 vector DNA was associated with blood cells following intratumoral injection during a clinical trial [34].…”

“…With respect to CAR affinity, the CAV-2 fiber head binds human CAR with the highest affinity of any fiber head known [24], which may favor its efficient hemagglutination. In contrast to other Ads, higher temperatures poorly inhibit CAV-2 hemagglutination [12], again suggesting a role for the high-affinity attachment to CAR. This is also consistent with a rather large difference between HAd5 and CAV-2 hemagglutination: to the best of our knowledge the HAd5 head does not harbor a sialic acid binding site and its pI (6.25) is less basic than HAd37 or CAV-2.…”

“…This highly heterogeneous lysate contains whole virus particles, empty capsids, penton monomers, penton dodecahedrons, fiber monomers, hexon etc. By using fractionated infected cell lysate, a handful of laboratories found that the multivalent complexes containing fiber were responsible for hemagglutination [9]–[12].…”

A human adenoviral vector with a chimeric fiber from canine adenovirus type 1 results in novel expanded tropism for cancer gene therapy

“…14 Another canine adenovirus strain, serotype 1 (CAV-1), has also been partially characterized. Whereas, its cell entry biology has not been described to the extent that has been accomplished for CAV-2, the pathological, structural, biophysical, and serological dissimilarities of CAV1 [19][20][21][22][23][24] in comparison to CAV-2 suggest that a distinct underlying tropism may be operational. In light of these considerations, we explored the potential utilization of an adenoviral xenotype possessing the fiber-knob of CAV-1.…”

Canine respiratory viruses

“…Vascular endothelial cells and hepatic and renal parenchymal cells are the main targets of CAV-1, while the respiratory tract epithelium and, to a limited degree, the intestinal epithelium, are the targets of CAV-2 [3,140,153]. In addition, the two types display different hemagglutination patterns [105].…”