caa a22 4500 475765826 CHVBK 20180406123605.0 cr unu---uuuuu 170329e20000601xx s 000 0 eng 10.1007/s007050070121 doi (NATIONALLICENCE)springer-10.1007/s007050070121 A conserved leucine in the cytoplasmic domain of the Semliki Forest virus spike protein is important for budding [Elektronische Daten] [U. Skoging-Nyberg, P. Liljeström] Summary.:  Budding of alphaviruses at the plasma membrane has been shown to depend on specific amino acids of the spike protein and hydrophobic cavities of the nucleocapsid. Here the function of leucine401 in the cytoplasmic tail of the Semliki Forest virus spike protein was studied. When alanine and threonine were substituted for leucine the budding efficiency decreased. When the alanine mutant virus was passaged and sequenced a valine residue at position 401 was found which could partially restore budding proficiency. These results show that leucine401 together with the previously identified tyrosine399 form a motif that is required for budding. Springer-Verlag/Wien, 2000 Skoging-Nyberg U. Microbiology and Tumorbiology Center, Karolinska Institute, Stockholm, Sweden, SE aut Liljeström P. Microbiology and Tumorbiology Center, Karolinska Institute, Stockholm, Sweden, SE aut https://doi.org/10.1007/s007050070121 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s007050070121 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Skoging-Nyberg U. Microbiology and Tumorbiology Center, Karolinska Institute, Stockholm, Sweden, SE aut NATIONALLICENCE 700 1- Liljeström P. Microbiology and Tumorbiology Center, Karolinska Institute, Stockholm, Sweden, SE aut Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer