Fielding incognito standardised patients as 'known' patients in a controlled trial in general practice.

Background: Incognito standardised patients (SPs) have only been used to represent new patients so far. The few trials with incognito SPs provide little detail on the method used for fielding them.

Objective: To establish the feasibility of introducing SPs as 'known' patients (i.

Visualization of the target-membrane-inserted fusion protein of Semliki Forest virus by combined electron microscopy and crystallography.

Semliki Forest virus enters cells by receptor-mediated endocytosis. The acidic environment of the endosome triggers a membrane fusion reaction that is mediated by the E1 glycoprotein. During fusion, E1 rearranges from an E1/E2 heterodimer to a highly stable, membrane-inserted E1 homotrimer (E1HT).

A zinc ion controls assembly and stability of the major capsid protein of rotavirus.

The recent determination of the crystal structure of VP6, the major capsid protein of rotavirus, revealed a trimer containing a central zinc ion coordinated by histidine 153 from each of the three subunits. The role of the zinc ion in the functions of VP6 was investigated by site-directed mutagenesis. The mutation of histidine 153 into a serine (H153S and H153S/S339H) did not prevent the formation of VP6 trimers.

Rotavirus nonstructural protein NSP5 interacts with major core protein VP2.

Rotavirus is a nonenveloped virus with a three-layered capsid. The inner layer, made of VP2, encloses the genomic RNA and two minor proteins, VP1 and VP3, with which it forms the viral core. Core assembly is coupled with RNA viral replication and takes place in definite cellular structures termed viroplasms.

The maturation process of pVP2 requires assembly of infectious bursal disease virus capsids.

Infectious bursal disease virus (IBDV) is a nonenveloped avian virus with a two-segment double-stranded RNA genome. Its T=13 icosahedral capsid is most probably assembled with 780 subunits of VP2 and 600 copies of VP3 and has a diameter of about 60 nm. VP1, the RNA-dependent RNA polymerase, resides inside the viral particle.