Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Hydrophobic photolabeling identifies BHA2 as the subunit mediating the interaction of bromelain-solubilized influenza virus hemagglutinin with liposomes at low pH

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00406a010· OSTI ID:6908812
To investigate the molecular basis of the low-pH-mediated interaction of the bromelain-solubilized ectodomain of influenza virus hemagglutinin (BHA) with membranes, we have photolabeled BHA in the presence of liposomes with the two carbene-generating, membrane-directed reagents 3-(trifluoromethyl)-3-(m-(/sup 125/I)iodophenyl)diazirine ((/sup 125/I)TID) and a new analogue of a phospholipid, 1-palmitoyl-2-(11-(4-(3-(trifluoromethyl)diazirinyl)phenyl)(2-/sup 3/H) undecanoyl)-sn-glycero-3-phosphocholine ((/sup 3/H)-PTPC/11). With the latter reagent, BHA was labeled in a strictly pH-dependent manner, i.e., at pH 5 only, whereas with (/sup 125/I)TID, labeling was seen also at pH 7. In all experiments, the label was selectively incorporated into the BHA2 polypeptide, demonstrating that the interaction of BHA with membranes is mediated through this subunit, possibly via its hydrophobic N-terminal segment. Similar experiments with a number of other water-soluble proteins (ovalbumin, carbonic anhydrase, alpha-lactalbumin, trypsin, and soybean trypsin inhibitor) indicate that the ability to interact with liposomes at low pH is not a property specific for BHA but is observed with other, perhaps most, proteins.
Research Organization:
Laboratorium fuer Biochemie der Eidgenoessischen Technischen Hochschule, Zuerich (Switzerland)
OSTI ID:
6908812
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 27:6; ISSN BICHA
Country of Publication:
United States
Language:
English