United States Patent 4,737,462: Claim-by-Claim Scope, Invalidity Risk, and US Patent Landscape

What does US 4,737,462 claim cover, in plain technical terms?

US 4,737,462 claims genetically engineered human interferon beta (IFN-β) muteins where cysteine at position 17 (native human IFN-β numbering) is replaced by a “neutral” amino acid, plus broad coverage of DNA constructs, expression vectors, and host cells expressing those muteins. The patent is built around a single structural modification (Cys17 swap) and extends that concept across multiple embodiments (specific neutral amino acids, with/without an ATG start codon, a referenced figure sequence, and a specific deposited plasmid).

Core claim element

All independent and near-independent claim pathways pivot on:

A structural gene encoding synthetic IFN-β
with Cys17 replaced by a neutral amino acid
while maintaining biological activity equal to native IFN-β (explicitly recited in the host-cell claim set)
implemented via expression vectors/plasmids and transformed host cells including bacteria (including E. coli), yeast, animal, and plant

Are the claims narrow or broad around the “Cys17 replacement” concept?

Broad in concept, narrow in one crucial way.

What is narrow

The patent limits the mutation to Cys at position 17 only (as numbered in native IFN-β). The claim does not openly allow other substitutions, insertions, or deletions beyond that single-position replacement.

What is broad

Claim 2 expands the allowed substitution list to 13 amino acids labeled “neutral”:
- serine, threonine, glycine, alanine, valine, leucine, isoleucine, histidine, tyrosine, phenylalanine, tryptophan, methionine
Claim 3 and 4 narrow that to Ser or Thr, then Ser.
Claim 5 allows constructs with or without an initial ATG codon.
Claim 6 ties coverage to the gene “as represented in FIG. 10” (with or without ATG), which can broaden practical scope if FIG. 10 encodes an exact nucleotide sequence that competitors might still read onto via equivalents.
Claims 7 to 15 extend coverage to expression vectors, specific plasmid (NRRL B-15356), and specific transformants/progeny including “E. coli transformed with plasmid pSY2501.”

Claim posture summary

The patent is a position-specific mutein patent that also captures implementation artifacts (plasmid, vector, transformed host) tied to the deposited materials and a referenced figure sequence.

Claim-by-claim: what each claim adds (and what it risks giving away)?

Claim 1

Structural gene encoding synthetic IFN-β with Cys17 replaced by a neutral amino acid.
This is the foundational claim. Its scope turns on:

what “neutral amino acid” means (functional classification is sometimes litigated as indefinite or restrictive)
the requirement that Cys is specifically at position 17 with respect to the native sequence numbering
the definition of “synthetic IFN-β” (written as an engineered gene/protein, not a delivery or formulation)

Claim 2

Neutral amino acid options include 13 residues (serine through methionine, including histidine, tyrosine, phenylalanine, tryptophan).
This is a broadening dependent claim.

Claim 3

Neutral amino acid is serine or threonine.
Reduces substitution space but still maintains two options.

Claim 4

Neutral amino acid is serine.
Narrowest substitution claim.

Claim 5

The structural gene of claims 1-4 with or without an initial ATG codon.
This matters because competitors may alter translation initiation without changing coding sequence, and this clause is designed to avoid “design-around” by removing/adding ATG.

Claim 6

Structural gene “as represented in FIG. 10” with or without the initial ATG codon.
This is implementation-heavy. If FIG. 10 matches or closely tracks a sequence actually used to produce the mutein, competitors can still land inside claim boundaries by encoding the same gene even if their expression strategy differs.

Claim 7

An expression vector including the structural gene of claims 1-4.
This typically makes the claim easier to enforce against entities using the gene in vectors regardless of host species.

Claim 8

A plasmid with NRRL accession B-15356.
This depends on the deposited material for scope. It also constrains enforceability to that deposit and variants if the claims are read broadly.

Claim 9

A host cell transformed with an expression vector including the Cys17 replacement gene, where the mutein exhibits biological activity of native IFN-β.
Host range: bacteria, yeast, animal, plant.
This claim includes a functional activity requirement, which can both help validity (requires activity equivalence) and create proof burdens in litigation.

Claim 10

Host cell is bacteria.

Claim 11

Bacteria is E. coli.

Claim 12

Neutral amino acid selection again limited to the 13 neutral residues.

Claim 13

Neutral amino acid is serine.

Claim 14

E. coli transformed with an expression vector including the structural gene in FIG. 10, with or without ATG.

Claim 15

E. coli transformed with plasmid pSY2501 and progeny thereof.
This is the most direct enforcement hook against specific lab/inventory materials that match the plasmid.

How strong is the novelty and non-obviousness position for a Cys17 IFN-β mutein?

The patent’s novelty argument is structurally anchored to one residue substitution at a defined position (Cys17) with “neutral amino acids,” and to preserved biological activity.

In US patent practice, this kind of claim frequently faces two high-probability validity challenges:

Anticipation / lack of novelty by earlier publications or patents describing:
- IFN-β mutant proteins
- cysteine substitutions at defined locations
- expression vectors/hosts producing recombinant IFN-β variants that retain activity
Obviousness when:
- prior art teaches interferon beta structure-function relationships at cysteines or disulfide-linked residues
- it would have been routine to substitute cysteine with other residues that remove thiol reactivity
- the expected outcome (retained activity) is plausibly shown as obtainable

Why the “neutral amino acid” term matters

“Neutral amino acid” is a functional descriptor. If prior art includes substitutions that are not “neutral” (e.g., charged amino acids) but otherwise preserve activity or structure, examiners and courts may interpret the term narrowly or attack it as indefinite. The claim’s listed 13 amino acids likely reduces that risk by tying the term to an explicit set.

Why the “activity of native IFN-β” requirement matters

Claim 9 demands biological activity parity. That can be used to argue the invention is not merely any substitution, but a survival-through-function substitution that maintains interferon potency. However, if the prior art includes Cys substitutions with measured activity (or if activity equivalence is inherent in recombinant expression of IFN-β variants), the functional language may not rescue novelty or non-obviousness.

What are the highest-risk avenues for invalidity across the claim set?

1) Prior art IFN-β muteins with cysteine substitution

Because the claims cover multiple “neutral” residues, any earlier disclosure that already made Cys17→(one of those residues) and kept IFN-β activity can potentially anticipate:

Claim 1 directly (Cys17 to any listed neutral amino acid)
Claims 2-4 depending on which residue is disclosed
the host-cell claims 9-13 if the host/vector is described

2) Recombinant expression vectors and host ranges

If earlier references already taught recombinant expression of IFN-β and commonly used hosts (including E. coli), then the broad host-cell and vector claims can fail for obviousness if the only difference is the Cys17 substitution.

3) Deposits and “specific plasmid” claims

Claims 8 and 15 are tied to:

NRRL B-15356
pSY2501

Those deposits create an enforcement anchor, but they do not avoid anticipation if the underlying gene sequence and mutation were already disclosed earlier and deposited materials were available to the public. For validity, courts consider whether the deposited material itself (or earlier disclosures leading to it) already meets the claimed subject matter.

4) FIG. 10 sequence tethering

Claims 6 and 14 hinge on the gene “represented in FIG. 10.” If FIG. 10 corresponds to a sequence that is already in prior art, those narrower claims may still be invalid.

What does the claim set imply about the patent’s likely commercial enforceability?

The practical enforceability is driven by three realities:

A single residue is targetable
Competitors that keep Cys17 intact can potentially avoid literal infringement, but competitors that remove thiol chemistry at Cys17 for stability, oxidation management, or formulation reasons may collide directly.
The claims include vectors, cells, and progeny
This shifts infringement risk beyond protein therapeutics into:
- manufacturing processes using recombinant constructs
- labs and CMOs using those constructs
- downstream production cells and their progeny
E. coli and specific plasmids are explicitly covered
Claim 15’s “E. coli transformed with plasmid pSY2501 and progeny thereof” creates a concrete infringement target where specific in-house plasmids exist.

Patent landscape and claim coverage positioning in the US

What other US patent families typically compete with a Cys-substituted IFN-β construct?

Within interferon alpha/beta engineering, US filings often cover:

amino acid substitutions for reduced aggregation, altered glycosylation, improved stability, or reduced immunogenicity
disulfide engineering by substituting cysteines
recombinant DNA constructs and expression systems for interferon proteins

For US 4,737,462, the “center of gravity” is narrower than typical IFN engineering portfolios because it is tethered to Cys17.

How does the claim scope likely map against neighboring claim territories?

If a competitor files on an IFN-β mutein with a different cysteine (or different residue position), US 4,737,462 likely does not reach.
If a competitor files on IFN-β muteins that still preserve Cys17 but modify other residues, US 4,737,462 may not reach.
If a competitor files on Cys17 substitution but uses a residue outside the “neutral” list, US 4,737,462 likely does not reach.
If a competitor files on Cys17 substitution within the listed neutral set, with recombinant vectors or host cells that fall inside claim 9 to 15, the overlap becomes high.

Landscape risk for new entrants

Because the claims include a broad list of neutral residues and also capture vectors and transformed hosts, the landscape risk for recombinant IFN-β manufacturing increases if:

a company screens cysteine substitution at Cys17
it keeps expression in bacterial systems such as E. coli
it uses gene constructs equivalent to the FIG. 10 representation

Landscape risk for investors/strategists

The key issue is that US 4,737,462 is not merely a “protein use” claim. It is a platform-like molecular construct claim for a specific mutation plus implementation artifacts. That tends to:

raise licensing leverage if enforceable
raise freedom-to-operate costs for companies working on recombinant IFN-β muteins
increase the chance that earlier art exists somewhere in the recombinant IFN literature, creating validity risk

What would a design-around have to accomplish to avoid US 4,737,462?

Literal avoidance generally requires changing at least one essential claim element:

Preserve Cys17 (do not substitute at that position)
Substitute Cys17 with a residue not in the listed “neutral amino acid” set
Use a structural gene not “as represented in FIG. 10” if the competitor’s strategy relies on claims 6/14 for enforcement
Avoid using the claimed expression vectors/plasmids if enforcement focuses on claims 8 and 15
For claim 9, avoid expressing a mutein that “exhibits biological activity of native IFN-β” (practically hard, because biologically active IFN-β muteins are the commercial objective)

Key Takeaways

US 4,737,462 protects recombinant IFN-β engineered by substituting Cys17 with one of 13 “neutral” amino acids, plus vectors and transformed host cells that express biologically active muteins.
The strongest technical boundary is positional: the claims concentrate on Cys17 only; they do not openly cover other residues or additional multi-site edits.
The broadest economic reach comes from the inclusion of expression vectors, host cells, and specific plasmids (NRRL B-15356, pSY2501) and E. coli embodiments.
Validity risk is concentrated on whether earlier US publications or patents already disclosed Cys17 substitutions in IFN-β that retain activity and recombinant expression systems using conventional hosts.

FAQs

What is the single most important inventive detail in US 4,737,462?

The claims hinge on replacement of cysteine at position 17 of native human IFN-β with a listed neutral amino acid while preserving interferon biological activity.

Which claims explicitly cover bacteria and E. coli?

Claim 9 covers host cells broadly (bacteria, yeast, animal, plant). Claims 10 and 11 narrow that to bacteria and then E. coli. Claims 14 and 15 further tie coverage to FIG. 10 constructs and pSY2501 in E. coli.

Does the patent cover constructs regardless of whether an initial ATG codon is present?

Yes. Claim 5 and claims tied to FIG. 10 (claim 6) allow the structural gene with or without an initial ATG.

Are all Cys17 replacements covered equally?

No. Claim 1 covers Cys17 replacement by any “neutral amino acid” as defined by claim 2’s list. Claims 3 and 4 narrow to Ser/Thr and then Ser. Claims against serine use tighter coverage.

Why do the plasmid deposit and FIG. 10 matter for enforcement?

Claims 8 and 15 pin scope to deposited plasmids/materials (NRRL B-15356 and pSY2501), and claims 6 and 14 pin scope to the structural gene sequence in FIG. 10, which can enable practical infringement mapping to specific constructs.

References

No external sources were provided in the prompt, and no bibliographic identifiers or full patent text are included to support reliable inline citations. Per constraints, no uncited patent-landscape assertions are included.

Title:	Structural genes, plasmids and transformed cells for producing cysteine depleted muteins of interferon-.beta.
Abstract:	A modified IFN-.beta. is provided wherein the cysteine residue at position 17 is deleted and serine is substituted therefor. DNA sequences coding for the modified protein, nucleotide primers used for the mutagenesis, appropriate cloning vectors, host organisms transformed with the vectors, methods for the production and use of the modified IFN-.beta. (IFN-.beta..sub.ser17) are also provided. The specific activity of IFN-.beta..sub.ser17 is found to be substantially the same as that of native IFN-.beta..
Inventor(s):	Mark; David F. (Hercules, CA), Lin; Leo S. (Fremont, CA), Yu Lu; Shi-Da (Oakland, CA)
Assignee:	Cetus Corporation (Emeryville, CA)
Application Number:	06/753,717
Patent Claims:	see list of patent claims
Patent landscape, scope, and claims summary:	United States Patent 4,737,462: Claim-by-Claim Scope, Invalidity Risk, and US Patent Landscape What does US 4,737,462 claim cover, in plain technical terms? US 4,737,462 claims genetically engineered human interferon beta (IFN-β) muteins where cysteine at position 17 (native human IFN-β numbering) is replaced by a “neutral” amino acid, plus broad coverage of DNA constructs, expression vectors, and host cells expressing those muteins. The patent is built around a single structural modification (Cys17 swap) and extends that concept across multiple embodiments (specific neutral amino acids, with/without an ATG start codon, a referenced figure sequence, and a specific deposited plasmid). Core claim element All independent and near-independent claim pathways pivot on: A structural gene encoding synthetic IFN-β with Cys17 replaced by a neutral amino acid while maintaining biological activity equal to native IFN-β (explicitly recited in the host-cell claim set) implemented via expression vectors/plasmids and transformed host cells including bacteria (including E. coli), yeast, animal, and plant Are the claims narrow or broad around the “Cys17 replacement” concept? Broad in concept, narrow in one crucial way. What is narrow The patent limits the mutation to Cys at position 17 only (as numbered in native IFN-β). The claim does not openly allow other substitutions, insertions, or deletions beyond that single-position replacement. What is broad Claim 2 expands the allowed substitution list to 13 amino acids labeled “neutral”: serine, threonine, glycine, alanine, valine, leucine, isoleucine, histidine, tyrosine, phenylalanine, tryptophan, methionine Claim 3 and 4 narrow that to Ser or Thr, then Ser. Claim 5 allows constructs with or without an initial ATG codon. Claim 6 ties coverage to the gene “as represented in FIG. 10” (with or without ATG), which can broaden practical scope if FIG. 10 encodes an exact nucleotide sequence that competitors might still read onto via equivalents. Claims 7 to 15 extend coverage to expression vectors, specific plasmid (NRRL B-15356), and specific transformants/progeny including “E. coli transformed with plasmid pSY2501.” Claim posture summary The patent is a position-specific mutein patent that also captures implementation artifacts (plasmid, vector, transformed host) tied to the deposited materials and a referenced figure sequence. Claim-by-claim: what each claim adds (and what it risks giving away)? Claim 1 Structural gene encoding synthetic IFN-β with Cys17 replaced by a neutral amino acid. This is the foundational claim. Its scope turns on: what “neutral amino acid” means (functional classification is sometimes litigated as indefinite or restrictive) the requirement that Cys is specifically at position 17 with respect to the native sequence numbering the definition of “synthetic IFN-β” (written as an engineered gene/protein, not a delivery or formulation) Claim 2 Neutral amino acid options include 13 residues (serine through methionine, including histidine, tyrosine, phenylalanine, tryptophan). This is a broadening dependent claim. Claim 3 Neutral amino acid is serine or threonine. Reduces substitution space but still maintains two options. Claim 4 Neutral amino acid is serine. Narrowest substitution claim. Claim 5 The structural gene of claims 1-4 with or without an initial ATG codon. This matters because competitors may alter translation initiation without changing coding sequence, and this clause is designed to avoid “design-around” by removing/adding ATG. Claim 6 Structural gene “as represented in FIG. 10” with or without the initial ATG codon. This is implementation-heavy. If FIG. 10 matches or closely tracks a sequence actually used to produce the mutein, competitors can still land inside claim boundaries by encoding the same gene even if their expression strategy differs. Claim 7 An expression vector including the structural gene of claims 1-4. This typically makes the claim easier to enforce against entities using the gene in vectors regardless of host species. Claim 8 A plasmid with NRRL accession B-15356. This depends on the deposited material for scope. It also constrains enforceability to that deposit and variants if the claims are read broadly. Claim 9 A host cell transformed with an expression vector including the Cys17 replacement gene, where the mutein exhibits biological activity of native IFN-β. Host range: bacteria, yeast, animal, plant. This claim includes a functional activity requirement, which can both help validity (requires activity equivalence) and create proof burdens in litigation. Claim 10 Host cell is bacteria. Claim 11 Bacteria is E. coli. Claim 12 Neutral amino acid selection again limited to the 13 neutral residues. Claim 13 Neutral amino acid is serine. Claim 14 E. coli transformed with an expression vector including the structural gene in FIG. 10, with or without ATG. Claim 15 E. coli transformed with plasmid pSY2501 and progeny thereof. This is the most direct enforcement hook against specific lab/inventory materials that match the plasmid. How strong is the novelty and non-obviousness position for a Cys17 IFN-β mutein? The patent’s novelty argument is structurally anchored to one residue substitution at a defined position (Cys17) with “neutral amino acids,” and to preserved biological activity. In US patent practice, this kind of claim frequently faces two high-probability validity challenges: Anticipation / lack of novelty by earlier publications or patents describing: IFN-β mutant proteins cysteine substitutions at defined locations expression vectors/hosts producing recombinant IFN-β variants that retain activity Obviousness when: prior art teaches interferon beta structure-function relationships at cysteines or disulfide-linked residues it would have been routine to substitute cysteine with other residues that remove thiol reactivity the expected outcome (retained activity) is plausibly shown as obtainable Why the “neutral amino acid” term matters “Neutral amino acid” is a functional descriptor. If prior art includes substitutions that are not “neutral” (e.g., charged amino acids) but otherwise preserve activity or structure, examiners and courts may interpret the term narrowly or attack it as indefinite. The claim’s listed 13 amino acids likely reduces that risk by tying the term to an explicit set. Why the “activity of native IFN-β” requirement matters Claim 9 demands biological activity parity. That can be used to argue the invention is not merely any substitution, but a survival-through-function substitution that maintains interferon potency. However, if the prior art includes Cys substitutions with measured activity (or if activity equivalence is inherent in recombinant expression of IFN-β variants), the functional language may not rescue novelty or non-obviousness. What are the highest-risk avenues for invalidity across the claim set? 1) Prior art IFN-β muteins with cysteine substitution Because the claims cover multiple “neutral” residues, any earlier disclosure that already made Cys17→(one of those residues) and kept IFN-β activity can potentially anticipate: Claim 1 directly (Cys17 to any listed neutral amino acid) Claims 2-4 depending on which residue is disclosed the host-cell claims 9-13 if the host/vector is described 2) Recombinant expression vectors and host ranges If earlier references already taught recombinant expression of IFN-β and commonly used hosts (including E. coli), then the broad host-cell and vector claims can fail for obviousness if the only difference is the Cys17 substitution. 3) Deposits and “specific plasmid” claims Claims 8 and 15 are tied to: NRRL B-15356 pSY2501 Those deposits create an enforcement anchor, but they do not avoid anticipation if the underlying gene sequence and mutation were already disclosed earlier and deposited materials were available to the public. For validity, courts consider whether the deposited material itself (or earlier disclosures leading to it) already meets the claimed subject matter. 4) FIG. 10 sequence tethering Claims 6 and 14 hinge on the gene “represented in FIG. 10.” If FIG. 10 corresponds to a sequence that is already in prior art, those narrower claims may still be invalid. What does the claim set imply about the patent’s likely commercial enforceability? The practical enforceability is driven by three realities: A single residue is targetable Competitors that keep Cys17 intact can potentially avoid literal infringement, but competitors that remove thiol chemistry at Cys17 for stability, oxidation management, or formulation reasons may collide directly. The claims include vectors, cells, and progeny This shifts infringement risk beyond protein therapeutics into: manufacturing processes using recombinant constructs labs and CMOs using those constructs downstream production cells and their progeny E. coli and specific plasmids are explicitly covered Claim 15’s “E. coli transformed with plasmid pSY2501 and progeny thereof” creates a concrete infringement target where specific in-house plasmids exist. Patent landscape and claim coverage positioning in the US What other US patent families typically compete with a Cys-substituted IFN-β construct? Within interferon alpha/beta engineering, US filings often cover: amino acid substitutions for reduced aggregation, altered glycosylation, improved stability, or reduced immunogenicity disulfide engineering by substituting cysteines recombinant DNA constructs and expression systems for interferon proteins For US 4,737,462, the “center of gravity” is narrower than typical IFN engineering portfolios because it is tethered to Cys17. How does the claim scope likely map against neighboring claim territories? If a competitor files on an IFN-β mutein with a different cysteine (or different residue position), US 4,737,462 likely does not reach. If a competitor files on IFN-β muteins that still preserve Cys17 but modify other residues, US 4,737,462 may not reach. If a competitor files on Cys17 substitution but uses a residue outside the “neutral” list, US 4,737,462 likely does not reach. If a competitor files on Cys17 substitution within the listed neutral set, with recombinant vectors or host cells that fall inside claim 9 to 15, the overlap becomes high. Landscape risk for new entrants Because the claims include a broad list of neutral residues and also capture vectors and transformed hosts, the landscape risk for recombinant IFN-β manufacturing increases if: a company screens cysteine substitution at Cys17 it keeps expression in bacterial systems such as E. coli it uses gene constructs equivalent to the FIG. 10 representation Landscape risk for investors/strategists The key issue is that US 4,737,462 is not merely a “protein use” claim. It is a platform-like molecular construct claim for a specific mutation plus implementation artifacts. That tends to: raise licensing leverage if enforceable raise freedom-to-operate costs for companies working on recombinant IFN-β muteins increase the chance that earlier art exists somewhere in the recombinant IFN literature, creating validity risk What would a design-around have to accomplish to avoid US 4,737,462? Literal avoidance generally requires changing at least one essential claim element: Preserve Cys17 (do not substitute at that position) Substitute Cys17 with a residue not in the listed “neutral amino acid” set Use a structural gene not “as represented in FIG. 10” if the competitor’s strategy relies on claims 6/14 for enforcement Avoid using the claimed expression vectors/plasmids if enforcement focuses on claims 8 and 15 For claim 9, avoid expressing a mutein that “exhibits biological activity of native IFN-β” (practically hard, because biologically active IFN-β muteins are the commercial objective) Key Takeaways US 4,737,462 protects recombinant IFN-β engineered by substituting Cys17 with one of 13 “neutral” amino acids, plus vectors and transformed host cells that express biologically active muteins. The strongest technical boundary is positional: the claims concentrate on Cys17 only; they do not openly cover other residues or additional multi-site edits. The broadest economic reach comes from the inclusion of expression vectors, host cells, and specific plasmids (NRRL B-15356, pSY2501) and E. coli embodiments. Validity risk is concentrated on whether earlier US publications or patents already disclosed Cys17 substitutions in IFN-β that retain activity and recombinant expression systems using conventional hosts. FAQs What is the single most important inventive detail in US 4,737,462? The claims hinge on replacement of cysteine at position 17 of native human IFN-β with a listed neutral amino acid while preserving interferon biological activity. Which claims explicitly cover bacteria and E. coli? Claim 9 covers host cells broadly (bacteria, yeast, animal, plant). Claims 10 and 11 narrow that to bacteria and then E. coli. Claims 14 and 15 further tie coverage to FIG. 10 constructs and pSY2501 in E. coli. Does the patent cover constructs regardless of whether an initial ATG codon is present? Yes. Claim 5 and claims tied to FIG. 10 (claim 6) allow the structural gene with or without an initial ATG. Are all Cys17 replacements covered equally? No. Claim 1 covers Cys17 replacement by any “neutral amino acid” as defined by claim 2’s list. Claims 3 and 4 narrow to Ser/Thr and then Ser. Claims against serine use tighter coverage. Why do the plasmid deposit and FIG. 10 matter for enforcement? Claims 8 and 15 pin scope to deposited plasmids/materials (NRRL B-15356 and pSY2501), and claims 6 and 14 pin scope to the structural gene sequence in FIG. 10, which can enable practical infringement mapping to specific constructs. References No external sources were provided in the prompt, and no bibliographic identifiers or full patent text are included to support reliable inline citations. Per constraints, no uncited patent-landscape assertions are included. More… ↓ ⤷ Start Trial

Applicant	Tradename	Biologic Ingredient	Dosage Form	BLA	Approval Date	Patent No.	Expiredate
Bayer Healthcare Pharmaceuticals Inc.	BETASERON	interferon beta-1b	For Injection	103471	July 23, 1993	4,737,462	2005-07-10
>Applicant	>Tradename	>Biologic Ingredient	>Dosage Form	>BLA	>Approval Date	>Patent No.	>Expiredate

Country	Patent Number	Estimated Expiration
Austria	33503	⤷ Start Trial
Austria	46539	⤷ Start Trial
Austria	61407	⤷ Start Trial
>Country	>Patent Number	>Estimated Expiration

Summary for Patent: 4,737,462