Cross-linking of phospholipids to proteins in the erythrocyte membrane

Marinetti, G.V.; Baumgarten, Ronald J.; Sheeley, D.; Gordesky, Stanley E.

doi:10.1016/0006-291x(73)91434-4

Cited by 27 publications

(11 citation statements)

References 8 publications

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“…Moreover, GA apparently selectively cross-links the nonglycoprotein components of the human erythrocyte membrane (2,48). DMA also acts predominantly on membrane proteins (25), but cross-links only the glycoproteins present in the membrane (20). Thus Not surprisingly, the conjugate-induced clustering can be blocked by pretreating the red cells with GA before conjugate staining (Fig.…”

Section: Discussionmentioning

confidence: 91%

The role of antigen mobility in anti-Rh0(D)-induced agglutination.

Victoria¹,

Muchmore²,

Sudora³

et al. 1975

J. Clin. Invest.

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Section: Discussionmentioning

confidence: 91%

The role of antigen mobility in anti-Rh0(D)-induced agglutination.

Victoria¹,

Muchmore²,

Sudora³

et al. 1975

J. Clin. Invest.

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“…Diimidoesters are mild crosslinking reagents that have been used to study intramolecular distances in protein molecules (27), subunit associations in oligorneric proteins (20), arrangement of ribosomal proteins (28,29), and protein-protein associations in the erythrocyte membrane (12,14,30). DMS can crosslink protein amino groups not further apart than 1i1 A (28).…”

Section: Nc-e Particles Containing ['H]leucine- ['H]isoleucine- Andmentioning

confidence: 99%

Location of the Spike Glycoproteins in the Semliki Forest Virus Membrane

Garoff

Simons

1974

Proc. Natl. Acad. Sci. U.S.A.

156

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Labeling experiments with formyl-[uS]-methionyl sulfone methylphosphate and crosslinking studies with dimethylsuberimidate suggest that the spike glycoproteins of Semliki Forest virus extend through the viral membrane into close contact with the nucleocapsid. Based on this finding, we present a mechanism for the formation of virus-specific patches in the host cell plasma membrane during virus assembly.We have been studying the membrane of Semliki Forest virus (SFV), a group A togavirus, to investigate the structure and assembly of biological membranes (1). SFV is composed of a smooth-surfaced nucleocapsid, which is surrounded by a lipid membrane (2, 3). The nucleocapsid is assembled in the cytoplasm of the host cell (2). It consists of the viral RNA and one lysine-rich protein species [molecular weight (MW) 33, 000] (4). The viral membrane is acquired from the host cell plasma membrane by a budding process in the final stage of SFV maturation (2). It has a lipid composition similar to that of the host cell plasma membrane (5), and its lipids seem to be arranged in a bilayer structure (6). Three virus-specific glycosylated proteins have been found in about equimolar ratios in the SFV membrane: El, E2 (both with a MW of about 50,000), and E3 (MW about 10,000) (H. Garoff, K.Simons, and 0. Renkonen, Virology, in press). The glycoproteins form spikes on the external surface of the bilayer, and are responsible for the hemagglutinating activity of the virus (7). The spikes can be cleaved off by thermolysin, leaving two hydrophobic peptides in the membrane derived from El and E2 (7). The peptides are large enough (MW about 5000 for each) to span the viral membrane like the intramembranous region of the MN glycoprotein (glycophorin) in the human erythrocyte membrane (8).Since no host cell proteins are found in the viral membrane of the mature virus particle, this membrane must be derived from a segment of the plasma membrane from which all host cell proteins are excluded (1). How such patches of viral membrane are generated is an enigma (9). In this report we present results suggesting that one or both of the viral spike glycoproteins El and E2 extend through the SFV membrane into close contact with the nucleocapsid. Based on this finding, a mechanism is presented that could explain the formation of virus-specific patches in the host cell plasma membrane, during virus assembly. of Na2CO3 buffer (pH 9.7) was mixed with 40 Mll of the [MS]-FMMP reagent and incubated at room temperature for 10 min. Excess reagent was removed by sucrose density gradient centrifugation (16). Viral membranes were released from another virus preparation containing 540 gg of protein by treatment with 170 j.g of Triton X-100 in 170 ul of the Na2CO3 buffer for 10 min at room temperature as described (17) before the labeling reagent (50 Md of ["S]FMMP) was added. The released membranes were separated from the nucleocapsids by centrifugation in a 15-30% (w/w) sucrose density gradient containing 0.1 M NaCl-0.05 M Tris buffer (pH 7.4) and 0.013...

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“…After 18 hr in 10% formalin, the erythrocytes were found to be resistant to a variety of treatments, as found by earlier workers using different bifunctional reagents (Berg et al, 1965;Dutton et al, 1966;Marinetti et al, 1973). The cells could withstand several rounds of extraction in mixtures of chloroform and methanol.…”

Section: Formaldehyde-fixed Cellsmentioning

confidence: 74%

ABO(H) blood group antigens of the human erythrocyte membrane: Contribution of glycoprotein and glycolipid

Mehta¹

1980

J. Membrain Biol.

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Formaldehyde-fixed human erythrocytes were extracted with sodium dodecyl sulfate and with three other solvent systems, at least two of which are known to remove glycolipids quantitatively. The extracted cells possessed the ability to absorb the ABO blood group-specific antibody at about one-third the level of unextracted cells. Treatment of fresh cells with pronase also reduced the ability of the cells to absorb the antibody, further supporting the presence of ABO blood group active glycoprotein in the membrane. Trypsinization of red cells, while removing PAS-1 and partly PAS-2, did not lead to any decrease in the activity. Papainization also did not diminish the activity, although PAS-1, PAS-2, and PAS-3 were removed from the cells. Thus, both glycolipid and glycoprotein contribute to ABO antigens of erythrocytes. Also, none of the three major glycoproteins of the membrane bears this activity.

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Cross-linking of phospholipids to proteins in the erythrocyte membrane

Cited by 27 publications

References 8 publications

The role of antigen mobility in anti-Rh0(D)-induced agglutination.

The role of antigen mobility in anti-Rh0(D)-induced agglutination.

Location of the Spike Glycoproteins in the Semliki Forest Virus Membrane

ABO(H) blood group antigens of the human erythrocyte membrane: Contribution of glycoprotein and glycolipid

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