Human papillomavirus type 16 E5 protein localizes to the Golgi apparatus but does not grossly affect cellular glycosylation

The E5 protein of papillomaviruses is a strongly hydrophobic membrane prote in that can associate with the 16 kDa protein subunit of the vacuolar proto n ATPase in endosomes and the Golgi apparatus resulting in raise of intraor ganelle pH. We demonstrate that E5 of human papillomavirus type 16 (HPV16) when transfected into human keratinocytes localizes to the Golgi. Using FAG S analysis and western blotting with a variety of lectins as well as analys ing the sialylation status of a specific cell surface glycoprotein CD95 (AP O-1/Fas), we show that HPV 16 E5 does not grossly affect cellular glycosyla tion, a main Golgi function.