Mengo virion

These results have been confirmed for the Mengo virion by electron microscopic examination of dissociating virus and size measurements of the isolated I4S and 5 products (55) (A similar model has been proposed for PMBV 1 56), but in this case dissociation by acidic pH occurs along the sides of icosahedral facets, creating trimers of (I/PI, 2, 3) which have a sedimentation coefficient of 12 and a molecular weight of 265,000). 

The spatial relationships of proteins in such complicated assemblies as ribosomes and membranes have been at least partially elucidated by reaction with bifunctional crosslinking reagents and subsequent analysis of the polypeptide composition of complexes by gel electrophoresis procedures (58) We have been using this approach to further probe the molecular anatomy of the Mengo virion and to attempt to answer some of the questions listed above. While such studies are not complete, some useful information has been obtained (59)-... 

Figure 2. Electron micrographs of (a) untreated Mengo virions (h) virions dissociated into 14 pentamers by incubation with 0.14 M 5 ( ) virions treated with DMA prior to...

These data have been incorporated into a schematic model of the Mengo virion which is presented in Figure J, The model is incomplete in that the location of the 6 polypeptides have not been established,nor have the interactions of the virion RNA with the capsid protein been determined. 

Figure 5 A model of the Mengo virion showing the relationships...

MAK> T.W., COLTER, J.S. and SCRABA, D.G. Structure of the Mengo virion. II. Physicoohemical and electron microscopic analysis of degraded virus. Virology (1974), 543-553. 

Figure 1 illustrates the results of an experiment where Mengo polypeptides in intact virions were crosslinked via free amino groups by dimethy1suberimidate. Subsequent separation, cleavage... 

Figure 1. Analysis of Mengo capsid protein complexes formed by the crosslinking reagent dimethylsuberimidate (DMS). H-amino acid-labeled virions were incubated with 20 DMS at room temperature for 24 hr, then disrupted by boiling in 2 sodium dodecylsulfate. Capsid proteins and higher-molecular weight complexes were separated by electrophoresis in SDS-containing polyacrylamide gels (60).

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