Purification and visualization of influenza a viral ribonucleoprotein complexes.

The influenza A viral genome consists of eight negative-sense, single stranded RNA molecules, individually packed with multiple copies of the influenza A nucleoprotein (NP) into viral ribonulceoprotein particles (vRNPs). The influenza vRNPs are enclosed within the viral envelope. During cell entry, however, these vRNP complexes are released into the cytoplasm, where they gain access to the host nuclear transport machinery.

Screening and characterization of surface-tethered cationic peptides for antimicrobial activity.

There is an urgent need to coat the surfaces of medical devices, including implants, with antimicrobial agents to reduce the risk of infection. A peptide array technology was modified to permit the screening of short peptides for antimicrobial activity while tethered to a surface. Cellulose-amino-hydroxypropyl ether (CAPE) linker chemistry was used to synthesize, on a cellulose support, peptides that remained covalently bound during biological assays.

Ultrastructural analysis of the nuclear localization sequences on influenza A ribonucleoprotein complexes.

The influenza A genome consists of eight single-stranded RNA molecules, each associated with an oligomeric core of the structural protein, nucleoprotein, to form a distinct viral ribonucleoprotein (vRNP) complex. vRNPs are the entities responsible for the transcription and replication of the influenza viral RNAs in the nuclei of host cells. Thus, nuclear targeting and localization of the vRNPs are a critical step in the infection and life cycle of influenza A.