Assembly of influenza hemagglutinin trimers and its role in intracellular transport

Journal Article · Wed Oct 01 04:00:00 EDT 1986 · J. Cell Biol.; (United States)

DOI:https://doi.org/10.1083/jcb.103.4.1179· OSTI ID:6437649

Copeland, C S; Doms, R W; Bolzau, E M; Webster, R G; Helenius, A

The hemagglutinin (HA) of influenza virus is a homotrimeric integral membrane glycoprotein. It is cotranslationally inserted into the endoplasmic reticulum as a precursor called HA0 and transported to the cell surface via the Golgi complex. The authors have, in this study, investigated the kinetics and cellular location of the assembly reaction that results in HA0 trimerization using (/sup 35/S)-methionine. Three independent criteria were used for determining the formation of quaternary structure: the appearance of an epitope recognized by trimer-specific monoclonal antibodies; the acquisition of trypsin resistance, a characteristic of trimers; and the formation of stable complexes which cosedimented with the mature Ha0 trimer (9S/sub 20,w/) in sucrose gradients containing triton X-100. The results showed that oligomer formation is a posttranslational event, occurring with a half time of approx.7.5 min after completion of synthesis. Assembly occurs in the endoplasmic reticulum, followed almost immediately by transport to the Golgi complex. A stabilization event in trimer structure occurs when HA0 leaves the Golgi complex or reaches the plasma membrane. Approximately 10% of the newly synthesized HA0 formed aberrant trimers which were not transported from the endoplasmic reticulum to the Golgi complex or the plasma membrane. Taken together the results suggested that formation of correctly folded quaternary structure constitutes a key event regulating the transport of the protein out of the endoplasmic reticulum. Further changes in subunit interactions occur as the trimers move along the secretory pathway.

• Research Organization: Yale Univ. School of Medicine, New Haven, CT
• OSTI ID: 6437649
• Journal Information: J. Cell Biol.; (United States), Journal Name: J. Cell Biol.; (United States) Vol. 103:4; ISSN JCLBA
• Country of Publication: United States
• Language: English

Related Subjects

550601* -- Medicine-- Unsealed Radionuclides in Diagnostics
62 RADIOLOGY AND NUCLEAR MEDICINE
AGGLUTININS
AMINO ACIDS
ANIMAL CELLS
ANTIBODIES
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOLOGY
BODY
CARBOXYLIC ACIDS
CELL CONSTITUENTS
CYTOLOGY
DAYS LIVING RADIOISOTOPES
DRUGS
ELECTRON CAPTURE RADIOISOTOPES
ELECTRON MICROSCOPY
ENDOPLASMIC RETICULUM
EVEN-ODD NUCLEI
FLUORESCENCE
HEMAGGLUTININS
INFLUENZA VIRUSES
INTERMEDIATE MASS NUCLEI
IODINE 125
IODINE ISOTOPES
ISOTOPES
KIDNEYS
LIGHT NUCLEI
LIPOTROPIC FACTORS
LUMINESCENCE
MEMBRANE PROTEINS
METHIONINE
MICROORGANISMS
MICROSCOPY
MOLECULAR BIOLOGY
MONOCLONAL ANTIBODIES
NUCLEI
ODD-EVEN NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
ORGANOIDS
ORGANS
PARASITES
PROTEINS
RADIOASSAY
RADIOISOTOPES
RECEPTORS
SULFUR 35
SULFUR ISOTOPES
VIRUSES