Disease relevance of VP35

• The nucleocapsid protein VP35 of Marburgvirus, a filovirus, acts as the cofactor of the viral polymerase and plays an essential role in transcription and replication of the viral RNA [1].
• Using salt dissociation of isolated virions, four proteins (NP, VP35, VP30, and L) remained attached to the core complex [2].

High impact information on VP35

• Thus, it is presumed that homo-oligomerization-negative mutants of VP35 are unable to recruit the polymerase to the NP/RNA template [1].
• Finally, transcriptionally inactive mutants of VP35 containing the functional homo-oligomerization domain displayed a dominant-negative phenotype [1].
• Substitution of leucine residues 90 and 104 abolished (i) the probability to form coiled coils, (ii) homo-oligomerization, and (iii) the function of VP35 in viral RNA synthesis [1].
• These data indicate that VP35, rather than VP30, is the functional homologue of rhabdo- and paramyxovirus P proteins [3].
• Results indicated that either GP or NP were protective antigens while VP35 afforded incomplete protection [4].

Biological context of VP35

• Using deletion mutants of L, the binding site of VP35 on L could be restricted to the N-terminal 530 amino-acid residues [2].
• To better define the genetic variation within the species, VP35 and glycoprotein (GP) genes of representative human isolates from four known episodes of Marburg virus hemorrhagic fever were analyzed [5].
• Small interfering RNAs (siRNAs) homologous to three MARV transcripts (NP, VP35 and VP30) were co-transfected into cells with plasmids encoding the corresponding nucleocapsid proteins [6].

Anatomical context of VP35

• In contrast, inability to homo-oligomerize did not abolish the recruitment of VP35 into inclusion bodies, which contain nucleocapsid-like structures formed by NP [1].
• B-cell epitopes were not found on the C-terminus of VP35 by use of PAbs or MAbs [7].

Other interactions of VP35

• These fragments were found to encode the VP35 and VP40 proteins [8].

Analytical, diagnostic and therapeutic context of VP35

• Northern blot analysis of viral RNA revealed that three nucleocapsid proteins (NP, VP35, and L) were essential and sufficient for transcription as well as replication and encapsidation [3].
• Two major sites on VP35 and a set of truncated VP35 fragments were found by use of an enzyme immunoassay and immunoblot [7].

References