Thèse numérisée par la Division de la gestion de documents et des archives de l'Université de Montréal.

Thèse numérisée par la Division de la gestion de documents et des archives de l'Université de Montréal

Thèse numérisée par la Direction des bibliothèques de l'Université de Montréal.

<p>IP-based TV (IPTV) is gradually replacing traditional means for broadcasting. At the same time, players from the telecom industry is seeking to create a new, standardized architectural framework for delivering all kinds of multimedia services over IP to end users; the IP Multimedia Subsystem (IMS).</p><p>This thesis is about video on demand, one of the more popular services enabled by IPTV. The thesis starts out by introducing the reader to IMS and IPTV and presents the current work in the area of IMS-based IPTV, done by the TISPAN committee of the ETSI.</p><p>The author then takes an explorative approach in investigating how a signaling schema for an IMS-based VOD service could look like, based on TISPAN’s existing work. The service is subject to an extra requirement; it should support session continuity, meaning it should be possible to resume the streaming of a video where the user left off, possibly on a different device. The investigation shows that it is possible to combine SIP and RTSP in several ways to get the desired behaviour.</p><p>The second part of the results consists of a proof of technology-implementation of the signaling schema that is the output from the first part. The implemented service runs on an IPTV set-top box on the client side, and a regular PC on the server side. The service uses open source software to a great extent and is fairly portable. A sample VOD session using the implemented system is presented along with full message contents.</p><p>The thesis concludes with a summary of the results and a discussion on what has been left out from the implementation and possibly subject to further studies. Finally, there is a brief summary on the recent developments within the field of IMS-based IPTV.</p>

IP-based TV (IPTV) is gradually replacing traditional means for broadcasting. At the same time, players from the telecom industry is seeking to create a new, standardized architectural framework for delivering all kinds of multimedia services over IP to end users; the IP Multimedia Subsystem (IMS). This thesis is about video on demand, one of the more popular services enabled by IPTV. The thesis starts out by introducing the reader to IMS and IPTV and presents the current work in the area of IMS-based IPTV, done by the TISPAN committee of the ETSI. The author then takes an explorative approach in investigating how a signaling schema for an IMS-based VOD service could look like, based on TISPAN’s existing work. The service is subject to an extra requirement; it should support session continuity, meaning it should be possible to resume the streaming of a video where the user left off, possibly on a different device. The investigation shows that it is possible to combine SIP and RTSP in several ways to get the desired behaviour. The second part of the results consists of a proof of technology-implementation of the signaling schema that is the output from the first part. The implemented service runs on an IPTV set-top box on the client side, and a regular PC on the server side. The service uses open source software to a great extent and is fairly portable. A sample VOD session using the implemented system is presented along with full message contents. The thesis concludes with a summary of the results and a discussion on what has been left out from the implementation and possibly subject to further studies. Finally, there is a brief summary on the recent developments within the field of IMS-based IPTV.

This master's thesis is focused on IPTV based on multicast technology. The main aim of this work is to provide detailed analysis of system for watching TV over IP network. It also describes components of IPTV architecture. This master's thesis also discussing about authentication and administration of settopboxes, deals with efficient distribution firmware for STB over multicast and tries to propose and implement portal which provides customer services. It describes the interface development as web service for interconnecting with another management, monitoring and billing information systems. The solution is implemented as a modul into an existing IS of commercial internet service provider.

Thèse numérisée par la Direction des bibliothèques de l'Université de Montréal.

Contention resolution coordinates access to a shared communication channel divided into synchronized slots. For any fixed slot, a packet can be sent, leading to three outcomes: empty (no packet sent), successful (one packet sent), or collision (multiple packets sent). Each slot provides ternary feedback: empty, successful, or collision. Much of the prior work has mainly focused on optimizing the makespan, the number of slots needed for all packets to succeed. However, in many modern systems, collisions also incur time costs, which existing algorithms do not address. In this thesis, we design and analyze a randomized contention-resolution algorithm, Collision-Evasion Backoff, that optimizes both the makespan and the cost of collisions. In our research, �� ≥ 2 packets are initially present in the system, and each collision has a known cost C, where 1 ≤ C ≤ ���� for a known ��. With error probability polynomially small in ��, Collision-Evasion Backoff guarantees that all packets succeed with makespan �� (��√C log(��)) and a total expected collision cost of �� (��√C log2 (��)).

Le gène de l’entérotoxine thermostable b (estB) d’Escherichia coli a été fusionné au gène de la protéine liant le maltose (malE) dans le vecteur pMAL-p via PCR. Par la suite, deux constructions plasmidiques ont été realisées à partir de ce nouveau vecteur, nommé pMAL-STb. Dans un premier temps, un marqueur hexahistidine (His6) a été ajouté entre malE et estB, et dans un deuxième temps, un marqueur décahistidine (His10) a été placé en amont de malE. La séquence signal de la protéine liant le maltose (MBP) dirige l’exportation de la protéine de fusion du cytoplasme vers le périplasme, où l’entérotoxine STb acquière sa conformation active. MBP est également reconnue pour améliorer le rendement et la solubilité de la protéine passagère tandis que le marqueur histidine, connu comme étant le meilleur marqueur d’affinité pour la purification protéique, facilite sa purification jusqu’à homogénéité. De plus, les gènes fusionnés sont sous le contrôle du promoteur tac (Ptac), un promoteur fort et inductible. Suite à l’induction par l’IPTG, la souche recombinante exprime une protéine d’environ 48 kDa, qui est facilement identifiable par électrophorèse à partir du surnageant obtenu via choc osmotique. Une séquence encodant un site de clivage spécifique au facteur Xa est présente dans le plasmide afin de séparer les marqueurs MBP et histidine de STb. Le clivage de la protéine de fusion avec le facteur Xa libère MBP (42 kDa) attachée au marqueur histidine et un polypeptide de 5.2 kDa, correspondant au poids moléculaire de STb mature. Avec cette méthode, nous visons à obtenir une méthode plus efficace pour la production et la purification de STb. / The heat-stable enterotoxin b gene (estB) of Escherichia coli was fused to the gene for maltose-binding protein (malE) into the pMAL-p vector using PCR. Afterward, two plasmid constructs were realized from this new vector, named pMAL-STb. Firstly, a hexahistidine tag (His6) was added between malE and estB and secondly, a decahistidine tag (His10) was placed upstream of malE. The signal sequence of maltose-binding protein (MBP) directs the export of the fusion protein from the cytoplasm to the periplasm, where the enterotoxin STb acquires its active conformation. MBP is also known to improve the yield and solubility of the passenger protein while the histidine tag, viewed as the best affinity tag for protein purification, facilitates its purification to homogeneity. Furthermore, the fused genes are controlled by the tac promoter (Ptac), a strong inducible promoter. Following IPTG induction, the recombinant strain expressed a protein of approximately 48 kDa, which is easily identified from osmotic shock fluid following electrophoresis. A sequence encoding a factor Xa cleavage site is present in the plasmid to separate MBP and histidine tags from STb. The cleavage of the fusion protein with factor Xa generates the maltose-binding protein (42 kDa) attached to the histidine tag and a polypeptide of 5.2 kDa, corresponding to the molecular mass of mature STb. With this method, we aim at obtaining a more efficient way to produce and purify STb.

Les E. coli entérotoxinogènes (ETEC) sont souvent la cause de diarrhée post-sevrage chez le porc. Deux types d’entérotoxines sont retrouvées chez les ETEC, soit les thermolabiles, comme la toxine LT, et les thermostables, comme EAST-1, STa et STb. Cette dernière est composée de 48 acides aminés et est impliquée dans la pathologie causée par les ETEC. Pour la première fois un variant de la toxine STb fut découvert dans une étude. Nous avons alors émis l’hypothèse qu’il y a présence de variants dans la population de souches ETEC du Québec. Dans les 100 souches STb+ analysées, 23 possédaient le gène de la toxine avec une variation dans la séquence génétique : l’asparagine était présente en position 12 remplaçant ainsi l’histidine. Une corrélation entre la présence du variant et la présence de facteurs de virulence retrouvés dans ces 100 souches ETEC étudiées a été effectuée. Ce variant semble fortement associé à la toxine STa puisque toutes les souches variantes ont hybridé avec le gène codant pour cette dernière. Étant donné sa présence répandue dans la population de souches ETEC du Québec, nous avons de plus émis l’hypothèse que ce variant a des caractéristiques biologiques altérées par rapport à la toxine sauvage. L’analyse par dichroïsme circulaire a montré que le variant et la toxine sauvage ont une structure secondaire ainsi qu’une stabilité similaires. Par la suite, l’attachement au récepteur de la toxine, le sulfatide, a été étudié par résonnance plasmonique de surface (biacore). Le variant a une affinité au sulfatide légèrement réduite comparativement à la toxine sauvage. Puisque l’internalisation de la toxine fut observée dans une étude précédente et qu’elle semble liée à la toxicité, nous avons comparé l’internalisation du variant et de la toxine sauvage à l’intérieur des cellules IPEC-J2. L’internalisation du variant dans les cellules est légèrement supérieure à l’internalisation de la toxine sauvage. Ces résultats suggèrent que le variant est biochimiquement et structurellement comparable à la toxine sauvage. / Enterotoxigenic Escherichia coli (ETEC) are a major cause of post-weaning diarrhea. STb is one of two heat-stable toxins produced by ETEC and is mostly associated with pathogenic porcine isolates. For the first time, a variant of the toxin was observed in a study in 2003. Our hypothesis is that STb variants are present in ETEC strains from Quebec. To screen for alterations at the gene level, a collection of 100 STb+ ETEC strains isolated from diseased pigs was randomly selected and analyzed. A total of 23 strains had a change from His12 to Asn. An association between the presence of the variant and virulence factors present in those strains was done. These strains were also positive for STa. Since this variant seems to be widely distributed in Quebec, we hypothesize that the variant has different biological properties compared to the wild-type STb. First, the secondary structure of the variant and wild-type toxin and their thermal stability was determined by circular dichroism. Both show similar structures and thermal stability. In addition, the binding affinity with the toxin receptor, the sulfatide, was determined by surface plasmon resonance. The affinity of the wild-type for the sulfatide is slightly superior to the variant. Finally, the internalization inside IPEC-J2 cells of the variant was compared to the wild-type. The variant is able to internalize more cells than the wild-type. Altogether, these results suggest that both the variant and the wild-type toxin are biochemically and structurally similar.