{'fraction_non_alphanumeric': 0.021370670596904937, 'fraction_numerical': 0.021370670596904937, 'mean_word_length': 4.853448275862069, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Early synthesis of Semliki Forest virus-specific proteins in infected chicken cells

Cells preinfected with fowl plague virus followed by treatment with actinomycin D are a suitable system for studying early protein synthesis in cells infected with Semliki forest virus. One and one-half hours after superinfection, three new nonstructural proteins (NVP) were detected: NVP 145, NVP, 112, and NVP 65. They appeared in parallel with a low incorporation of mannose at the beginning of the infectious cycle. Behavior on chasing suggested a precursor relationship of NVP 112 to the envelope glycoproteins. Two kinds of NVP 65 are described, both of which are varieties of NVP 68 with an incomplete mannose content. One type, detected early after infection, was converted into NVP 68 by supplementary glycosylation. The second, late type was stable. It contains fucose and resembles the NVP 65 observed after impairment of glycosylation. The mechanism of NVP 68 glycosylation is discussed. The presence of the complete carbohydrate moiety is crucial for the cleavage of NVP 68 into the envelope proteins E2 and E3 and, thus, for virus maturation. Only the complete form of NVP 68 was precipitated by envelope-specific antisera. A large production of NVP 78 is a further feature of the early events in infected cells. It is not related to the structural proteins.