A CXCR4/CD4 Pseudotype Rhabdovirus That Selectively Infects HIV-1 Envelope Protein-Expressing Cells

نویسندگان

  • Teshome Mebatsion
  • Stefan Finke
  • Frank Weiland
  • Karl-Klaus Conzelmann
چکیده

We show that a cellular virus receptor functions in the envelope of a virus, allowing selective infection of cells displaying the receptor ligand. A G-deficient rabies virus (RV) pseudotyped with CD4- and CXCR4-derived proteins selectively infected cells expressing HIV-1 envelope protein. Envelope protein or CD4 antibodies blocked virus entry. Pseudotype virus formation was most efficient with chimeric receptor proteins possessing the cytoplasmic tail of the RV G spike protein (CXCR4-RV and CD4-RV). While CXCR4-RV was incorporated when expressed alone, CD4-RV incorporation required CXCR4-RV as a carrier protein, indicating a mechanism by which oligomeric surface proteins are sorted into the RV envelope. Viral vectors bearing virus receptors in their envelope may be useful reagents for targeting virus-infected cells in vivo.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Infection of cells expressing CXCR4 mutants lacking N-glycosylation at the N-terminal extracellular domain is enhanced for R5X4-dualtropic human immunodeficiency virus type-1

BACKGROUND Infection with human immunodeficiency virus type-1 (HIV-1) requires binding of the viral envelope gp120 to CD4 and to the CXCR4 coreceptor. Both, gp120 and CXCR4 are subject to N-glycosylation. Here we investigated the influence of the N-linked glycans g1 and g2 present on CXCR4 for HIV-1 infection. METHODS The two CXCR4 N-glycosylation sites g1 (NYT) and g2 (NVS) were mutated by c...

متن کامل

Thermal Stability of the Human Immunodeficiency Virus Type 1 (HIV-1) Receptors, CD4 and CXCR4, Reconstituted in Proteoliposomes

BACKGROUND The entry of human immunodeficiency virus (HIV-1) into host cells involves the interaction of the viral exterior envelope glycoprotein, gp120, and receptors on the target cell. The HIV-1 receptors are CD4 and one of two chemokine receptors, CCR5 or CXCR4. METHODOLOGY/PRINCIPAL FINDINGS We created proteoliposomes that contain CD4, the primary HIV-1 receptor, and one of the corecepto...

متن کامل

Title Raft localization of CXCR 4 is primarily required for X 4 - tropic

Human immunodeficiency virus type 1 (HIV-1) infection is initiated by successive interactions of viral envelope glycoprotein gp120 with two cellular surface proteins, CD4 and chemokine receptor. The two most common chemokine receptors that allow HIV-1 entry are the CCR5 and CXCR4. The CD4 and CCR5 are mainly localized to the particular plasma membrane microdomains, termed raft, which is rich in...

متن کامل

CXCR4/fusin Is Not a Species-specific Barrier in Murine Cells for HIV-1 Entry

Since some murine cells expressing human CD4 fail to internalize HIV-1, another block was thought to be located at the level of viral entry in addition to CD4. Recently, CXCR4 was shown to function as a coreceptor for T cell line-tropic HIV-1 entry. Here we demonstrated that cells expressing murine CXCR4 and human CD4 fused with cells expressing the env proteins derived from T cell line-tropic ...

متن کامل

Adaptation of the human immunodeficiency virus type 1 envelope glycoproteins to new world monkey receptors.

Human immunodeficiency virus type 1 (HIV-1) infection encounters an early block in the cells of New World monkeys because the CD4 receptor does not efficiently support HIV-1 entry. We adapted HIV-1(NL4-3) and HIV-1(KB9), two HIV-1 variants with different envelope glycoproteins, to replicate efficiently in cells expressing the CD4 and CXCR4 proteins of the common marmoset, a New World monkey. Th...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Cell

دوره 90  شماره 

صفحات  -

تاریخ انتشار 1997