Specific inhibition of paramyxovirus and myxovirus replication by oligopeptides with amino acid sequences similar to those at the N-termini of the Fl or HA2 viral polypeptides

Richardson, Christopher D.; Scheid, Andreas; Choppin, Purnell W.

doi:10.1016/0042-6822(80)90168-3

Cited by 356 publications

(209 citation statements)

References 35 publications

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“…In both cases, virus attachment was not affected. In the case of the tripeptide analogue (116-118), it has been proposed that this prevents fusion by competing with the fusion protein for a cellular receptor (Richardson et al, 1980). However, escape mutants that resist the effect of the tripeptide were found to possess mutations in the cysteine-rich region of MV F (Hull et al, 1987), which we have shown to be the site of interaction with the MV HA (T. F. Wild et al, 1994).…”

Section: Discussionmentioning

confidence: 99%

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Inhibition of measles virus infection and fusion with peptides corresponding to the leucine zipper region of the fusion protein.

Wild

Buckland

1997

Journal of General Virology

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Section: Discussionmentioning

confidence: 99%

“…Peptides representing two different regions of the MV F protein, amino acids 116-118 (Norrby, 1971 ;Richardson et al, 1980) and 455-490, have been shown to inhibit fusion. In both cases, virus attachment was not affected.…”

Section: Discussionmentioning

confidence: 99%

Inhibition of measles virus infection and fusion with peptides corresponding to the leucine zipper region of the fusion protein.

Wild

Buckland

1997

Journal of General Virology

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“…On the other hand, the natural cleavage of SeV F protein into F2 and F1 occurs between the R and F in Figure 1b, and the resulting N-terminal sequence of the F1 begins with FFG. A previous study demonstrated that the carbobenzoxy-FFG oligopeptide could specifically inhibit SeV fusion activity and infectivity in cultured cells, 26 suggesting that the N-terminal FFG was specifically required for fusion capacity. Thus, the addition of LGL or LWA to the natural N-terminal FFG might impair fusion activity.…”

Section: Cell-to-cell Spreading Of M Gene-deleted Sevmentioning

confidence: 97%

Generation of a recombinant Sendai virus that is selectively activated and lyses human tumor cells expressing matrix metalloproteinases

et al. 2004

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Malignant tumor cells often express matrix metalloproteinases (MMPs) at a high level to enable their dissemination and metastasis. Sendai virus (SeV), a nonsegmented negative strand RNA virus, spreads in the target tissues in vivo via cleavage activation of the viral fusion glycoprotein by a tissue-specific, trypsin-like enzyme. By deleting the viral matrix protein, we previously generated a recombinant SeV that does not bud to mature virions, but is highly fusogenic and spreads extensively from cell to cell in a trypsindependent manner. Here, we changed the tryptic cleavage site of the fusion glycoprotein of this virus to a site susceptible to MMPs. The resulting recombinant virus was no longer activated by trypsin but spread efficiently in cultured cells supplemented with MMP2 or MMP9 and in human tumor cell lines expressing these MMPs. Furthermore, the virus spread extensively in tumor cells xenotrasplanted to nude mice without disseminating to the surrounding normal cells, leading to the inhibition of the tumor growth in the mice. These results demonstrate the selective targeting and killing of human tumor cells by recombinant SeV technology and greatly advance the reemerging concept of oncolytic virotherapy, which currently appears to rely largely upon a natural preference of certain viruses for cancer cells.

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“…Syncytia and eGFP expression were analyzed 2d post-infection using a DMIL microscope with a DFC320 camera (Leica Microsystems). For flowcytometry, the fusion inhibitory peptide Z-D-Phe-l-Phe-l-Gly (FIP [54]) (0.2 mM) (Bachem) was added. After 2d, cells were stained with anti-MV-F.…”

Section: Infectionmentioning

confidence: 99%

Human Langerhans cells capture measles virus through Langerin and present viral antigens to CD4⁺ T cells but are incapable of cross‐presentation

et al. 2011

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Langerhans cells (LCs) are a subset of DCs that reside in the upper respiratory tract and are ideally suited to sense respiratory virus infections. Measles virus (MV) is a highly infectious lymphotropic and myelotropic virus that enters the host via the respiratory tract. Here, we show that human primary LCs are capable of capturing MV through the C-type lectin Langerin. Both immature and mature LCs presented MV-derived antigens in the context of HLA class II to MV-specific CD4 1 T cells. Immature LCs were not susceptible to productive infection by MV and did not present endogenous viral antigens in the context of HLA class I. In contrast, mature LCs could be infected by MV and presented de novo synthesized viral antigens to MV-specific CD8 1 T cells. Notably, neither immature nor mature LCs were able to cross-present exogenous UV-inactivated MV or MV-infected apoptotic cells. The lack of direct infection of immature LCs, and the inability of both immature and mature LCs to crosspresent MV antigens, suggest that human LCs may not be directly involved in priming MV-specific CD8 1 T cells. Immune activation of LCs seems a prerequisite for MV infection of LCs and subsequent CD8 1 T-cell priming via the endogenous antigen presentation pathway. Eur. J. Immunol. 2011. 41: 2619-2631 DOI 10.1002 Immunity to infection 2619 molecules, a process referred to as cross-presentation which is thought to be important in both viral and tumor immunity [2,3]. It is becoming evident that different DC subsets have specialized functions in anti-viral immunity, e.g. by inducing preferentially CD4 1 or CD8 1 T-cell responses or by inducing innate immunity against pathogens [4,5]. Langerhans cells (LCs) are a subset of DCs that are, in humans, characterized by expression of CD1a, the C-type lectin Langerin and the presence of Birbeck granules [6]. LCs reside in the epidermis and stratified epithelial tissues [7][8][9]. Recently, we have shown that LCs form a barrier against HIV-1; LCs capture HIV-1 through Langerin, resulting in internalization of HIV-1 into Birbeck granules and preventing subsequent HIV-1 transmission [10]. However, little is known about the role of human LCs and Langerin in antigen presentation.Capture of exogenous antigens by LCs leads to induction of CD4 1 T-cell responses [11][12][13]. However, the ability of LCs to cross-present exogenous antigens to CD8 1 T cells has been debated [14][15][16][17]. Klechevsky et al. [13] have shown that in vitrogenerated human LCs from either CD34 1 cells or monocytes are capable of cross-presenting influenza-virus proteins to CD8 1 T cells. However, these in vitro-generated LCs might be different from primary immature LCs.Here, we have investigated the antigen capture and presentation capacity of human primary LCs during measles virus (MV) infection. MV is the causative agent of measles, which remains an important cause of morbidity and mortality in developing countries. MV is a lymphotropic and myelotropic virus and DCs have been implicated in its transmission [18,19]. MV is on...

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Specific inhibition of paramyxovirus and myxovirus replication by oligopeptides with amino acid sequences similar to those at the N-termini of the Fl or HA2 viral polypeptides

Cited by 356 publications

References 35 publications

Inhibition of measles virus infection and fusion with peptides corresponding to the leucine zipper region of the fusion protein.

Inhibition of measles virus infection and fusion with peptides corresponding to the leucine zipper region of the fusion protein.

Generation of a recombinant Sendai virus that is selectively activated and lyses human tumor cells expressing matrix metalloproteinases

Human Langerhans cells capture measles virus through Langerin and present viral antigens to CD4⁺ T cells but are incapable of cross‐presentation

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Specific inhibition of paramyxovirus and myxovirus replication by oligopeptides with amino acid sequences similar to those at the N-termini of the Fl or HA2 viral polypeptides

Cited by 356 publications

References 35 publications

Inhibition of measles virus infection and fusion with peptides corresponding to the leucine zipper region of the fusion protein.

Inhibition of measles virus infection and fusion with peptides corresponding to the leucine zipper region of the fusion protein.

Generation of a recombinant Sendai virus that is selectively activated and lyses human tumor cells expressing matrix metalloproteinases

Human Langerhans cells capture measles virus through Langerin and present viral antigens to CD4+ T cells but are incapable of cross‐presentation

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Human Langerhans cells capture measles virus through Langerin and present viral antigens to CD4⁺ T cells but are incapable of cross‐presentation