Requirement of Calmodulin Binding by HIV-1 gp160 for Enhanced FAS-mediated Apoptosis

Micoli, Keith; Pan, George; Wu, Yong; Williams, John P.; Cook, William J.; McDonald, Jay M.

doi:10.1074/jbc.275.2.1233

Cited by 48 publications

(54 citation statements)

References 50 publications

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“…HIV-infected persons might have increased susceptibility to apoptosis because the HIV proteins Tat and Nef may induce endothelial cell apoptosis (49). It is also possible that HIV may cause apoptosis directly (50,51). It has been proposed that apoptosis, oxidative stress, and inflammation work in concert to promote COPD, and this scenario may be true in HIV-associated COPD as well (37).…”

Section: Apoptosismentioning

confidence: 99%

“…Organ-specific autoimmunity has been demonstrated as a complication of ART and seems to occur later than infection-associated IRIS (59,60). An increase in autoimmune conditions has also been noted in HIV-infected persons after beginning ART (4,(51)(52)(53)(54). Detectable antithyroid antibodies appear after initiation of ART, and clinical thyroid disease is associated with a lower pre-ART CD41 cell count (61,62).…”

Section: Effects Of Antiretroviral Therapymentioning

confidence: 99%

See 1 more Smart Citation

HIV and Chronic Obstructive Pulmonary Disease: Is It Worse and Why?

Morris¹,

George²,

Crothers³

et al. 2011

Proceedings of the American Thoracic Society

110

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Section: Apoptosismentioning

confidence: 99%

Section: Effects Of Antiretroviral Therapymentioning

confidence: 99%

HIV and Chronic Obstructive Pulmonary Disease: Is It Worse and Why?

Morris¹,

George²,

Crothers³

et al. 2011

Proceedings of the American Thoracic Society

110

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“…The ICD-TM region of HIV-1 and SIVmac has been implicated in proteinprotein interactions during virion assembly (14,23), cell surface expression of envelope (8,40,65), cell-cell fusion (62,72,85), induction of cytopathology (52,74), and apoptosis (50,58), perhaps related to binding of calmodulin (50,73,76,77).…”

mentioning

confidence: 99%

Live, Attenuated Simian Immunodeficiency Virus SIVmac-M4, with Point Mutations in the Env Transmembrane Protein Intracytoplasmic Domain, Provides Partial Protection from Mucosal Challenge with Pathogenic SIVmac251

Shacklett

Shaw

Adamson

et al. 2002

J Virol

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Attenuated molecular clones of simian immunodeficiency virus (SIVmac) are important tools for studying the correlates of protective immunity to lentivirus infection in nonhuman primates. The most highly attenuated SIVmac mutants fail to induce disease but also fail to induce immune responses capable of protecting macaques from challenge with pathogenic virus. We recently described a novel attenuated virus, SIVmac-M4, containing multiple mutations in the transmembrane protein (TM) intracytoplasmic domain. This domain has been implicated in viral assembly, infectivity, and cytopathogenicity. Whereas parental SIVmac239-Nef ؉ T-cell responses to Gag after challenge but not before. Unvaccinated control animals challenged with SIVmac251 developed persistent viremia, had significantly weaker SIV-specific T-cell responses, and developed AIDS-related symptoms. These findings demonstrate that SIVmac-M4, which contains a full-length Nef coding region and multiple point mutations in the TM, can provide substantial protection from mucosal challenge with pathogenic SIVmac251.

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“…In contrast to most viral glycoproteins, which have only short C-terminal domains, most lentiviral glycoproteins have long cytoplasmic C termini (150 to 200 aa). The functions of these conserved regions during wild-type virus infection have not been completely elucidated but may, in part, involve binding to calmodulin (26,40). Bulky heterologous C termini have been implicated to be inhibitory to incorporation and pseudotyping in many (15,24,37,44) but apparently not all (18) cases.…”

mentioning

confidence: 99%

Properties of Wild-Type, C-Terminally Truncated, and Chimeric Maedi-Visna Virus Glycoprotein and Putative Pseudotyping of Retroviral Vector Particles

Zeilfelder

Bosch

2001

J Virol

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We have characterized the properties of the maedi-visna virus (MVV) glycoprotein, which has a long cytoplasmic C-terminal domain, and of a panel of C-terminally truncated and C-terminally chimeric MVV-Env constructs. Cells expressing wild-type MVV glycoprotein form syncytia with target cells from many different species and tissues, demonstrating that the MVV-Env cellular receptor is widely distributed. Similar to the situation with other lentiviral glycoproteins, truncation of the C-terminal domain of MVV-Env significantly increases its membrane fusion capacity. However, despite their presence in a fusogenic form at the cell surface, neither the wild-type nor any of the C-terminally modified MVV-Env constructs, these latter lacking sterically inhibitory C termini, were able to successfully pseudotype murine leukemia virus-or human immunodeficiency virus-derived vector particles.The molecular processes which play a role in determining whether a particular surface glycoprotein can be incorporated into the membrane of retroviral particles and mediate virus infectivity are not yet entirely understood. Incorporation is not restricted to the homologous glycoprotein, and pseudotyping of retroviral vector particles can be achieved with a number of heterologous glycoproteins (e.g., the glycoproteins of amphotropic murine leukemia virus [MuLV-Env], vesicular stomatitis virus [VSV-G], and gibbon ape leukemia virus give rise to high vector titers on the order of 10 5 to 10 6 IU/ml). Further examples of pseudotyping include the use of the glycoproteins of Ebola virus (45), lymphocytic choriomeningitis virus (27), and fowl plague virus (hemagglutinin) (8, 13). Additionally, incorporation of several cellular glycoproteins into retroviral and rhabdoviral particles has been demonstrated directly elsewhere (1,10,14,15,25,36,47). In several instances in which the incorporated proteins represent cellular receptors for virus uptake, the pseudotyped virus particles were infectious for cells expressing the respective viral glycoprotein (1,10,25,36).All of these results demonstrate that foreign C-terminal regions on incorporated viral or cellular glycoproteins can be compatible with retroviral particle infectivity. However, it is of note that the naturally occurring C termini on these incorporable viral and cellular glycoproteins are usually relatively short (in the range of 15 to 35 amino acids [aa]). In contrast to most viral glycoproteins, which have only short C-terminal domains, most lentiviral glycoproteins have long cytoplasmic C termini (150 to 200 aa). The functions of these conserved regions during wild-type virus infection have not been completely elucidated but may, in part, involve binding to calmodulin (26, 40). Bulky heterologous C termini have been implicated to be inhibitory to incorporation and pseudotyping in many (15, 24, 37, 44) but apparently not all (18) cases. Thus, wildtype human immunodeficiency virus (HIV) glycoprotein, with its naturally occurring long C terminus (151 aa), was not able to pseudotype murine r...

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Requirement of Calmodulin Binding by HIV-1 gp160 for Enhanced FAS-mediated Apoptosis

Cited by 48 publications

References 50 publications

HIV and Chronic Obstructive Pulmonary Disease: Is It Worse and Why?

HIV and Chronic Obstructive Pulmonary Disease: Is It Worse and Why?

Live, Attenuated Simian Immunodeficiency Virus SIVmac-M4, with Point Mutations in the Env Transmembrane Protein Intracytoplasmic Domain, Provides Partial Protection from Mucosal Challenge with Pathogenic SIVmac251

Properties of Wild-Type, C-Terminally Truncated, and Chimeric Maedi-Visna Virus Glycoprotein and Putative Pseudotyping of Retroviral Vector Particles

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