The present study was undertaken to investigate the role of 'antigen processing' in influenza virus-specific cytotoxic T (Tc)-cell recognition. H-2 Db-restricted Tc-cell clones specific for the 1934 influenza nucleoprotein (NP) were tested in an in vitro proliferation assay for the recognition of intact virus, purified protein or peptide antigen. Inactivated virus required further 'processing', which was inhibited by either NH4Cl treatment or paraformaldehyde fixation of antigen-presenting cells (APC). Purified NP, by contrast, was readily presented by both normal peritoneal exudate cells and H-2 Db gene 'transfected' L cells. The response was not inhibited by either NH4Cl or prior paraformaldehyde treatment of APC. Peptone-induced peritoneal exudate cells presented ineffectively unless treated with NH4Cl or prefixed with paraformaldehyde. Comparison of the responses to either purified protein or a synthetic peptide implies that the epitope recognized by the three NP specific clones is not 'cryptic' and, therefore, that the purified protein, in this case, does not require 'processing'.